Explanation of inconsistencies in the determination of human serum albumin thermal stability
Thermal denaturation of human serum albumin has been the subject of many studies in recent decades, but the results of these studies are often conflicting and inconclusive. To clarify this, we combined different spectroscopic and calorimetric techniques and performed an in-depth analysis of the stru...
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| Published in | International journal of biological macromolecules Vol. 232; p. 123379 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
31.03.2023
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| Abstract | Thermal denaturation of human serum albumin has been the subject of many studies in recent decades, but the results of these studies are often conflicting and inconclusive. To clarify this, we combined different spectroscopic and calorimetric techniques and performed an in-depth analysis of the structural changes that occur during the thermal unfolding of different conformational forms of human serum albumin. Our results showed that the inconsistency of the results in the literature is related to the different quality of samples in different batches, methodological approaches and experimental conditions used in the studies. We confirmed that the presence of fatty acids (FAs) causes a more complex process of the thermal denaturation of human serum albumin. While the unfolding pathway of human serum albumin without FAs can be described by a two-step model, consisting of subsequent reversible and irreversible transitions, the thermal denaturation of human serum albumin with FAs appears to be a three-step process, consisting of a reversible step followed by two consecutive irreversible transitions.
•Thermal stability of albumin samples varies from batch to batch.•Thermal denaturation of albumin is a kinetically controlled multi-step process.•The presence of FAs causes a more complex thermal denaturation of albumin.•The thermal stability of albumin is strongly pH-dependent, even within a single conformational form. |
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| AbstractList | Thermal denaturation of human serum albumin has been the subject of many studies in recent decades, but the results of these studies are often conflicting and inconclusive. To clarify this, we combined different spectroscopic and calorimetric techniques and performed an in-depth analysis of the structural changes that occur during the thermal unfolding of different conformational forms of human serum albumin. Our results showed that the inconsistency of the results in the literature is related to the different quality of samples in different batches, methodological approaches and experimental conditions used in the studies. We confirmed that the presence of fatty acids (FAs) causes a more complex process of the thermal denaturation of human serum albumin. While the unfolding pathway of human serum albumin without FAs can be described by a two-step model, consisting of subsequent reversible and irreversible transitions, the thermal denaturation of human serum albumin with FAs appears to be a three-step process, consisting of a reversible step followed by two consecutive irreversible transitions. Thermal denaturation of human serum albumin has been the subject of many studies in recent decades, but the results of these studies are often conflicting and inconclusive. To clarify this, we combined different spectroscopic and calorimetric techniques and performed an in-depth analysis of the structural changes that occur during the thermal unfolding of different conformational forms of human serum albumin. Our results showed that the inconsistency of the results in the literature is related to the different quality of samples in different batches, methodological approaches and experimental conditions used in the studies. We confirmed that the presence of fatty acids (FAs) causes a more complex process of the thermal denaturation of human serum albumin. While the unfolding pathway of human serum albumin without FAs can be described by a two-step model, consisting of subsequent reversible and irreversible transitions, the thermal denaturation of human serum albumin with FAs appears to be a three-step process, consisting of a reversible step followed by two consecutive irreversible transitions.Thermal denaturation of human serum albumin has been the subject of many studies in recent decades, but the results of these studies are often conflicting and inconclusive. To clarify this, we combined different spectroscopic and calorimetric techniques and performed an in-depth analysis of the structural changes that occur during the thermal unfolding of different conformational forms of human serum albumin. Our results showed that the inconsistency of the results in the literature is related to the different quality of samples in different batches, methodological approaches and experimental conditions used in the studies. We confirmed that the presence of fatty acids (FAs) causes a more complex process of the thermal denaturation of human serum albumin. While the unfolding pathway of human serum albumin without FAs can be described by a two-step model, consisting of subsequent reversible and irreversible transitions, the thermal denaturation of human serum albumin with FAs appears to be a three-step process, consisting of a reversible step followed by two consecutive irreversible transitions. Thermal denaturation of human serum albumin has been the subject of many studies in recent decades, but the results of these studies are often conflicting and inconclusive. To clarify this, we combined different spectroscopic and calorimetric techniques and performed an in-depth analysis of the structural changes that occur during the thermal unfolding of different conformational forms of human serum albumin. Our results showed that the inconsistency of the results in the literature is related to the different quality of samples in different batches, methodological approaches and experimental conditions used in the studies. We confirmed that the presence of fatty acids (FAs) causes a more complex process of the thermal denaturation of human serum albumin. While the unfolding pathway of human serum albumin without FAs can be described by a two-step model, consisting of subsequent reversible and irreversible transitions, the thermal denaturation of human serum albumin with FAs appears to be a three-step process, consisting of a reversible step followed by two consecutive irreversible transitions. •Thermal stability of albumin samples varies from batch to batch.•Thermal denaturation of albumin is a kinetically controlled multi-step process.•The presence of FAs causes a more complex thermal denaturation of albumin.•The thermal stability of albumin is strongly pH-dependent, even within a single conformational form. |
| ArticleNumber | 123379 |
| Author | Fabriciová, Gabriela Nemergut, Michal Sedlák, Erik Sedláková, Dagmar Jancura, Daniel Belej, Dominik |
| Author_xml | – sequence: 1 givenname: Michal surname: Nemergut fullname: Nemergut, Michal organization: Center for Interdisciplinary Biosciences, P. J. Šafárik University in Košice, Jesenná 5, 04154 Košice, Slovakia – sequence: 2 givenname: Dagmar surname: Sedláková fullname: Sedláková, Dagmar organization: Department of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Košice, Slovakia – sequence: 3 givenname: Gabriela surname: Fabriciová fullname: Fabriciová, Gabriela organization: Department of Biophysics, Faculty of Science, P. J. Šafárik University in Košice, Jesenná 5, 04154 Košice, Slovakia – sequence: 4 givenname: Dominik surname: Belej fullname: Belej, Dominik organization: Department of Biophysics, Faculty of Science, P. J. Šafárik University in Košice, Jesenná 5, 04154 Košice, Slovakia – sequence: 5 givenname: Daniel surname: Jancura fullname: Jancura, Daniel organization: Department of Biophysics, Faculty of Science, P. J. Šafárik University in Košice, Jesenná 5, 04154 Košice, Slovakia – sequence: 6 givenname: Erik surname: Sedlák fullname: Sedlák, Erik email: erik.sedlak@upjs.sk organization: Center for Interdisciplinary Biosciences, P. J. Šafárik University in Košice, Jesenná 5, 04154 Košice, Slovakia |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/36702231$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1016/S0021-9258(18)37941-9 10.1046/j.1537-2995.1982.22583017454.x 10.1016/j.bbagen.2013.05.017 10.1002/chir.20709 10.1021/acsomega.8b00967 10.1016/j.bpc.2016.11.006 10.1590/S0100-879X1998001100003 10.1016/j.bpj.2014.10.055 10.1016/S0141-8130(96)01153-1 10.1016/0005-2760(79)90001-8 10.1021/acs.molpharmaceut.7b00976 10.1111/j.1751-1097.1973.tb06422.x 10.1038/358209a0 10.1007/BF02547420 10.1016/j.jinorgbio.2017.05.016 10.1016/j.ab.2005.12.029 10.1111/j.1467-8276.2006.00887.x 10.1039/C4RA09892G 10.1039/b808938h 10.1046/j.1432-1327.1999.00810.x 10.1021/acs.molpharmaceut.6b00277 10.1021/acs.jctc.5b01001 10.1023/A:1011932516717 10.1016/S0021-9258(19)37601-X 10.1007/s10973-005-7170-1 10.1016/j.jmb.2005.07.075 10.3390/nano6060116 10.1016/j.jphotobiol.2008.01.001 10.1002/pro.2691 10.1006/jmbi.2000.4158 10.1111/j.1399-3011.1976.tb02478.x 10.1038/1869 10.1021/la5034959 10.1016/j.jconrel.2015.06.006 10.1021/acs.jpclett.1c03735 10.1007/s13318-015-0297-y 10.1006/jmbi.2000.5208 10.1021/jp409936v 10.1016/j.ijbiomac.2017.04.051 10.1016/S1388-1981(99)00148-1 10.1002/(SICI)1097-0134(20000701)40:1<29::AID-PROT50>3.0.CO;2-P 10.1016/j.bbapap.2005.04.001 10.1016/j.ijbiomac.2015.02.003 10.1111/j.1432-1033.1980.tb04449.x 10.1021/acs.molpharmaceut.6b01124 10.1021/ja01207a034 10.1042/bj2580199 10.1002/pro.3278 10.1093/protein/12.6.439 10.1021/pr034094y 10.1111/j.1423-0410.1984.tb00096.x 10.1023/A:1011000317042 10.1186/s12938-019-0624-7 10.1002/1439-7633(20011105)2:11<813::AID-CBIC813>3.0.CO;2-W 10.1073/pnas.0806431105 10.1016/j.ijbiomac.2018.11.053 10.1007/BF01412043 10.1016/j.mam.2011.12.002 10.1016/S0006-3495(98)77598-8 10.1111/j.1423-0410.1984.tb01558.x 10.15171/apb.2016.063 10.1016/0305-0491(86)90215-4 10.1016/S0167-4838(02)00212-1 10.5483/BMBRep.2006.39.5.530 10.1074/jbc.275.5.3042 10.1016/j.molliq.2022.119042 10.1016/j.ijbiomac.2021.10.095 10.1016/j.bpc.2010.03.001 10.1016/S0006-3495(92)81899-4 10.1021/jp055989w 10.1080/19420862.2018.1450126 10.1016/j.colsurfb.2014.09.044 10.7150/thno.22069 10.3390/molecules26010108 |
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| Keywords | Thermodynamic and kinetic stability Protein thermal stability Serum albumin Phase diagram method Lumry-Eyring model |
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| References | Brandt, Andersson (bb0345) 1976; 8 Khashkhashi-Moghadam, Ezazi-Toroghi, Kamkar-Vatanparast, Jouyaeian, Mokaberi, Yazdyani, Amiri-Tehranizadeh, Reza Saberi, Chamani (bb0040) 2022; 356 Honoré, Pedersen (bb0160) 1989; 258 Michnik, Michalik, Kluczewska, Drzazga (bb0320) 2006; 84 Sugio, Kashima, Mochizuki, Noda, Kobayashi (bb0095) 1999; 12 Lahiri, Sandhu, Levine, Dantus (bb0270) 2022; 13 Bhattacharya, Prajapati, Chatterjee, Mukherjee (bb0280) 2014; 30 Sedlák, Ziegler, Kosman, Wittung-Stafshede (bb0330) 2008; 105 Aoki, Sakurai, Murata, Ito, Terada, Hiramatsu (bb0335) 1984; 262 Varshney, Sen, Ahmad, Rehan, Subbarao, Khan (bb0050) 2010; 22 Yu, Finlayson (bb0360) 1984; 47 Kuznetsova, Turoverov, Uversky (bb0300) 2004; 3 Curry, Mandelkow, Brick, Franks (bb0115) 1998; 5 Ross, Shrake (bb0340) 1988; 263 Nemergut, Zoldak, Schaefer, Kast, Miskovsky, Pluckthun, Sedlak (bb0390) 2017; 26 Sengupta, Das, Sen (bb0255) 2017; 221 Celej, Dassie, González, Bianconi, Fidelio (bb0325) 2006; 350 Ahmad, Muteeb, Alam, Varshney, Zaidi, Ishtikhar, Badr, Mahmoud, Khan (bb0235) 2015; 75 Ascenzi, Fasano (bb0110) 2010; 148 Qi, Zhang, Gou, Lee, Wang, Chen, Zhou, Wu, Yang, Liang (bb0025) 2016; 13 S. D, Lr (bb0060) 2013; 1830 Bhattacharya, Grüne, Curry (bb0100) 2000; 303 Cohn, Strong, Hughes, Mulford, Ashworth, Melin, Taylor (bb0165) 1946; 68 Schaefer, Sedlak, Kast, Nemergut, Pluckthun (bb0395) 2018; 10 Feng, Zhao, Wang, Qu, Zhu, Yang, An, Tian, Shou (bb0065) 2018; 8 Rabbani, Ahn (bb0080) 2019; 123 Lomis, Westfall, Farahdel, Malhotra, Shum-Tim, Prakash (bb0055) 2016; 6 Bern, Sand, Nilsen, Sandlie, Andersen (bb0070) 2015; 211 Raoufinia, Mota, Keyhanvar, Safari, Shamekhi, Abdolalizadeh (bb0180) 2016; 6 Bushmarina, Kuznetsova, Biktashev, Turoverov, Uversky (bb0290) 2001; 2 Ishtikhar, Rabbani, Khan (bb0145) 2014; 123 Gerety, Aronson (bb0185) 1982; 22 He, Carter (bb0090) 1992; 358 Ahmad, Ahmed, Haq, Khan (bb0210) 2005; 1750 Petitpas, Grüne, Bhattacharya, Curry (bb0105) 2001; 314 Leggio, Galantini, Pavel (bb0125) 2008; 10 Fanali, di Masi, Trezza, Marino, Fasano, Ascenzi (bb0010) 2012; 33 Sedlák, Varhač, Musatov, Robinson (bb0265) 2014; 107 Qu, Sun, Li, Hao, Qiu, Teng, Xie, Gao (bb0200) 2019; 18 Darcel, Kaldy (bb0190) 1986; 85 Rabbani, Baig, Lee, Cho, Ma, Choi (bb0305) 2017; 14 Farruggia, Rodriguez, Rigatuso, Fidelio, Picó (bb0315) 2001; 20 Baler, Martin, Carignano, Ameer, Vila, Szleifer (bb0140) 2014; 118 Díaz, Suárez (bb0155) 2016; 12 Barone, Capasso, Vecchio, Sena, Fessas, Giancola, Graziano, Tramonti (bb0195) 1995; 45 Dockal, Carter, Rüker (bb0130) 2000; 275 Qiu, Zhang, Okobiah, Yang, Wang, Zhong, Zewail (bb0135) 2006; 110 Mohan, Sengupta, Acharyya, Yadav, Das, Sen (bb0245) 2018; 3 Rezaei-Tavirani, Moghaddamnia, Ranjbar, Amani, Marashi (bb0240) 2006; 39 Curry, Brick, Franks (bb0120) 1999; 1441 Shrake, Finlayson, Ross (bb0355) 1984; 47 Shaw, Pal (bb0380) 2008; 90 Abdollahpour, Soheili, Saberi, Chamani (bb0035) 2016; 41 Sedlák, Schaefer, Marek, Gimeson, Plückthun (bb0260) 2015; 24 Gumpen, Hegg, Martens (bb0350) 1979; 574 Belej, Jurasekova, Nemergut, Wagnieres, Jancura, Huntosova (bb0030) 2017; 174 Foster (bb0005) 1977 Wetzel, Becker, Behlke, Billwitz, Böhm, Ebert, Hamann, Krumbiegel, Lassmann (bb0215) 1980; 104 Shrake, Ross (bb0365) 1988; 263 Sudlow, Birkett, Wade (bb0045) 1975; 11 Ghuman, Zunszain, Petitpas, Bhattacharya, Otagiri, Curry (bb0015) 2005; 353 Sanchez-Ruiz (bb0225) 1992; 61 Kuznetsova, Stepanenko, Turoverov, Zhu, Zhou, Fink, Uversky (bb0295) 2002; 1596 Rabbani, Ahn (bb0085) 2021; 193 Kosa, Maruyama, Otagiri (bb0250) 1998; 15 Muzammil, Kumar, Tayyab (bb0370) 1999; 266 Anand, Mukherjee (bb0275) 2013; 1830 Tanaka, Shigueoka, Sawatani, Dias, Arashiro, Campos, Nakao (bb0175) 1998; 31 Burstein, Vedenkina, Ivkova (bb0375) 1973; 18 Flora, Brennan, Baker, Doody, Bright (bb0230) 1998; 75 Rabbani, Baig, Jan, Ju Lee, Khan, Zaman, Farouk, Khan, Choi (bb0310) 2017; 105 Ishtikhar, Rabbani, Khan, Khan (bb0150) 2015; 5 Muzammil, Kumar, Tayyab (bb0205) 2000; 40 Kostandini, Mills, Norton (bb0020) 2006; 88 Edsall (bb0170) 1984; 46 Rabbani, Lee, Ahmad, Baig, Choi (bb0075) 2018; 15 Picó (bb0220) 1997; 20 Chubarov, Spitsyna, Krumkacheva, Mitin, Suvorov, Tormyshev, Fedin, Bowman, Bagryanskaya (bb0285) 2021; 26 Peters (bb0385) 1996 Kuznetsova (10.1016/j.ijbiomac.2023.123379_bb0300) 2004; 3 Gumpen (10.1016/j.ijbiomac.2023.123379_bb0350) 1979; 574 Gerety (10.1016/j.ijbiomac.2023.123379_bb0185) 1982; 22 Farruggia (10.1016/j.ijbiomac.2023.123379_bb0315) 2001; 20 Bern (10.1016/j.ijbiomac.2023.123379_bb0070) 2015; 211 Bushmarina (10.1016/j.ijbiomac.2023.123379_bb0290) 2001; 2 Baler (10.1016/j.ijbiomac.2023.123379_bb0140) 2014; 118 He (10.1016/j.ijbiomac.2023.123379_bb0090) 1992; 358 Shrake (10.1016/j.ijbiomac.2023.123379_bb0365) 1988; 263 Rabbani (10.1016/j.ijbiomac.2023.123379_bb0305) 2017; 14 Michnik (10.1016/j.ijbiomac.2023.123379_bb0320) 2006; 84 Anand (10.1016/j.ijbiomac.2023.123379_bb0275) 2013; 1830 Sedlák (10.1016/j.ijbiomac.2023.123379_bb0330) 2008; 105 Honoré (10.1016/j.ijbiomac.2023.123379_bb0160) 1989; 258 Feng (10.1016/j.ijbiomac.2023.123379_bb0065) 2018; 8 Muzammil (10.1016/j.ijbiomac.2023.123379_bb0370) 1999; 266 Curry (10.1016/j.ijbiomac.2023.123379_bb0120) 1999; 1441 Petitpas (10.1016/j.ijbiomac.2023.123379_bb0105) 2001; 314 Sanchez-Ruiz (10.1016/j.ijbiomac.2023.123379_bb0225) 1992; 61 Ross (10.1016/j.ijbiomac.2023.123379_bb0340) 1988; 263 Raoufinia (10.1016/j.ijbiomac.2023.123379_bb0180) 2016; 6 Belej (10.1016/j.ijbiomac.2023.123379_bb0030) 2017; 174 Flora (10.1016/j.ijbiomac.2023.123379_bb0230) 1998; 75 Chubarov (10.1016/j.ijbiomac.2023.123379_bb0285) 2021; 26 Picó (10.1016/j.ijbiomac.2023.123379_bb0220) 1997; 20 Rabbani (10.1016/j.ijbiomac.2023.123379_bb0310) 2017; 105 Darcel (10.1016/j.ijbiomac.2023.123379_bb0190) 1986; 85 Shrake (10.1016/j.ijbiomac.2023.123379_bb0355) 1984; 47 Nemergut (10.1016/j.ijbiomac.2023.123379_bb0390) 2017; 26 Rabbani (10.1016/j.ijbiomac.2023.123379_bb0080) 2019; 123 Burstein (10.1016/j.ijbiomac.2023.123379_bb0375) 1973; 18 Aoki (10.1016/j.ijbiomac.2023.123379_bb0335) 1984; 262 Kosa (10.1016/j.ijbiomac.2023.123379_bb0250) 1998; 15 Tanaka (10.1016/j.ijbiomac.2023.123379_bb0175) 1998; 31 Qu (10.1016/j.ijbiomac.2023.123379_bb0200) 2019; 18 Kuznetsova (10.1016/j.ijbiomac.2023.123379_bb0295) 2002; 1596 Ishtikhar (10.1016/j.ijbiomac.2023.123379_bb0145) 2014; 123 Varshney (10.1016/j.ijbiomac.2023.123379_bb0050) 2010; 22 Sedlák (10.1016/j.ijbiomac.2023.123379_bb0260) 2015; 24 Díaz (10.1016/j.ijbiomac.2023.123379_bb0155) 2016; 12 Ghuman (10.1016/j.ijbiomac.2023.123379_bb0015) 2005; 353 Rabbani (10.1016/j.ijbiomac.2023.123379_bb0075) 2018; 15 Leggio (10.1016/j.ijbiomac.2023.123379_bb0125) 2008; 10 Sedlák (10.1016/j.ijbiomac.2023.123379_bb0265) 2014; 107 S. D (10.1016/j.ijbiomac.2023.123379_bb0060) 2013; 1830 Curry (10.1016/j.ijbiomac.2023.123379_bb0115) 1998; 5 Fanali (10.1016/j.ijbiomac.2023.123379_bb0010) 2012; 33 Sudlow (10.1016/j.ijbiomac.2023.123379_bb0045) 1975; 11 Dockal (10.1016/j.ijbiomac.2023.123379_bb0130) 2000; 275 Sugio (10.1016/j.ijbiomac.2023.123379_bb0095) 1999; 12 Abdollahpour (10.1016/j.ijbiomac.2023.123379_bb0035) 2016; 41 Schaefer (10.1016/j.ijbiomac.2023.123379_bb0395) 2018; 10 Lomis (10.1016/j.ijbiomac.2023.123379_bb0055) 2016; 6 Brandt (10.1016/j.ijbiomac.2023.123379_bb0345) 1976; 8 Shaw (10.1016/j.ijbiomac.2023.123379_bb0380) 2008; 90 Ahmad (10.1016/j.ijbiomac.2023.123379_bb0210) 2005; 1750 Celej (10.1016/j.ijbiomac.2023.123379_bb0325) 2006; 350 Barone (10.1016/j.ijbiomac.2023.123379_bb0195) 1995; 45 Kostandini (10.1016/j.ijbiomac.2023.123379_bb0020) 2006; 88 Qiu (10.1016/j.ijbiomac.2023.123379_bb0135) 2006; 110 Ahmad (10.1016/j.ijbiomac.2023.123379_bb0235) 2015; 75 Sengupta (10.1016/j.ijbiomac.2023.123379_bb0255) 2017; 221 Bhattacharya (10.1016/j.ijbiomac.2023.123379_bb0280) 2014; 30 Edsall (10.1016/j.ijbiomac.2023.123379_bb0170) 1984; 46 Mohan (10.1016/j.ijbiomac.2023.123379_bb0245) 2018; 3 Muzammil (10.1016/j.ijbiomac.2023.123379_bb0205) 2000; 40 Peters (10.1016/j.ijbiomac.2023.123379_bb0385) 1996 Wetzel (10.1016/j.ijbiomac.2023.123379_bb0215) 1980; 104 Khashkhashi-Moghadam (10.1016/j.ijbiomac.2023.123379_bb0040) 2022; 356 Ishtikhar (10.1016/j.ijbiomac.2023.123379_bb0150) 2015; 5 Lahiri (10.1016/j.ijbiomac.2023.123379_bb0270) 2022; 13 Ascenzi (10.1016/j.ijbiomac.2023.123379_bb0110) 2010; 148 Foster (10.1016/j.ijbiomac.2023.123379_bb0005) 1977 Qi (10.1016/j.ijbiomac.2023.123379_bb0025) 2016; 13 Bhattacharya (10.1016/j.ijbiomac.2023.123379_bb0100) 2000; 303 Cohn (10.1016/j.ijbiomac.2023.123379_bb0165) 1946; 68 Rabbani (10.1016/j.ijbiomac.2023.123379_bb0085) 2021; 193 Yu (10.1016/j.ijbiomac.2023.123379_bb0360) 1984; 47 Rezaei-Tavirani (10.1016/j.ijbiomac.2023.123379_bb0240) 2006; 39 |
| References_xml | – volume: 148 start-page: 16 year: 2010 end-page: 22 ident: bb0110 article-title: Allostery in a monomeric protein: the case of human serum albumin publication-title: Biophys. Chem. – volume: 26 start-page: 108 year: 2021 ident: bb0285 article-title: Reversible dimerization of human serum albumin publication-title: Molecules – volume: 174 start-page: 37 year: 2017 end-page: 44 ident: bb0030 article-title: Negligible interaction of [Ru(Phen)3]2+ with human serum albumin makes it promising for a reliable in vivo assessment of the tissue oxygenation publication-title: J. Inorg. Biochem. – volume: 5 start-page: 827 year: 1998 end-page: 835 ident: bb0115 article-title: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites publication-title: Nat. Struct. Biol. – volume: 11 start-page: 824 year: 1975 end-page: 832 ident: bb0045 article-title: The characterization of two specific drug binding sites on human serum albumin publication-title: Mol. Pharmacol. – volume: 13 start-page: 3098 year: 2016 end-page: 3105 ident: bb0025 article-title: Multidrug delivery systems based on human serum albumin for combination therapy with three anticancer agents publication-title: Mol. Pharm. – volume: 2 start-page: 813 year: 2001 end-page: 821 ident: bb0290 article-title: Partially folded conformations in the folding pathway of bovine carbonic anhydrase II: a fluorescence spectroscopic analysis publication-title: Chembiochem – start-page: 53 year: 1977 end-page: 84 ident: bb0005 article-title: Some aspects of the structure and conformational properties of serum albumin publication-title: Albumin: Structure, Function and Uses – volume: 3 start-page: 485 year: 2004 end-page: 494 ident: bb0300 article-title: Use of the phase diagram method to analyze the protein unfolding-refolding reactions: fishing out the “invisible” intermediates publication-title: J. Proteome Res. – volume: 303 start-page: 721 year: 2000 end-page: 732 ident: bb0100 article-title: Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin publication-title: J. Mol. Biol. – volume: 18 start-page: 263 year: 1973 end-page: 279 ident: bb0375 article-title: Fluorescence and the location of tryptophan residues in protein molecules publication-title: Photochem. Photobiol. – volume: 356 year: 2022 ident: bb0040 article-title: Novel perspective into the interaction behavior study of the cyanidin with human serum albumin-holo transferrin complex: spectroscopic, calorimetric and molecular modeling approaches publication-title: J. Mol. Liq. – volume: 30 start-page: 14894 year: 2014 end-page: 14904 ident: bb0280 article-title: Concentration-dependent reversible self-oligomerization of serum albumins through intermolecular β-sheet formation publication-title: Langmuir – volume: 105 start-page: 19258 year: 2008 end-page: 19263 ident: bb0330 article-title: In vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 15 start-page: 1445 year: 2018 end-page: 1456 ident: bb0075 article-title: Binding of tolperisone hydrochloride with human serum albumin: effects on the conformation, thermodynamics, and activity of HSA publication-title: Mol. Pharm. – volume: 314 start-page: 955 year: 2001 end-page: 960 ident: bb0105 article-title: Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids publication-title: J. Mol. Biol. – volume: 275 start-page: 3042 year: 2000 end-page: 3050 ident: bb0130 article-title: Conformational transitions of the three recombinant domains of human serum albumin depending on pH publication-title: J. Biol. Chem. – volume: 14 start-page: 1656 year: 2017 end-page: 1665 ident: bb0305 article-title: Biophysical study on the interaction between eperisone hydrochloride and human serum albumin using spectroscopic, calorimetric, and molecular docking analyses publication-title: Mol. Pharm. – volume: 13 start-page: 1825 year: 2022 end-page: 1832 ident: bb0270 article-title: Human serum albumin dimerization enhances the S2 emission of bound cyanine IR806 publication-title: J. Phys. Chem. Lett. – volume: 1596 start-page: 138 year: 2002 end-page: 155 ident: bb0295 article-title: Unraveling multistate unfolding of rabbit muscle creatine kinase publication-title: Biochim. Biophys. Acta – volume: 15 start-page: 449 year: 1998 end-page: 454 ident: bb0250 article-title: Species differences of serum albumins: II. Chemical and thermal stability publication-title: Pharm. Res. – volume: 24 start-page: 1100 year: 2015 end-page: 1113 ident: bb0260 article-title: Advanced analyses of kinetic stabilities of iggs modified by mutations and glycosylation publication-title: Protein Sci. – volume: 1441 start-page: 131 year: 1999 end-page: 140 ident: bb0120 article-title: Fatty acid binding to human serum albumin: new insights from crystallographic studies publication-title: Biochim. Biophys. Acta – volume: 6 start-page: 116 year: 2016 ident: bb0055 article-title: Human serum albumin nanoparticles for use in cancer drug delivery: process optimization and in vitro characterization publication-title: Nanomaterials (Basel) – volume: 10 start-page: 6741 year: 2008 end-page: 6750 ident: bb0125 article-title: About the albumin structure in solution: cigar expanded form versus heart Normal shape publication-title: Phys. Chem. Chem. Phys. – volume: 1830 start-page: 5394 year: 2013 end-page: 5404 ident: bb0275 article-title: Binding, unfolding and refolding dynamics of serum albumins publication-title: Biochim. Biophys. Acta Gen. Subj. – volume: 263 start-page: 11196 year: 1988 end-page: 11202 ident: bb0340 article-title: Decrease in stability of human albumin with increase in protein concentration publication-title: J. Biol. Chem. – volume: 353 start-page: 38 year: 2005 end-page: 52 ident: bb0015 article-title: Structural basis of the drug-binding specificity of human serum albumin publication-title: J. Mol. Biol. – volume: 3 start-page: 10406 year: 2018 end-page: 10417 ident: bb0245 article-title: Region-specific double denaturation of human serum albumin: combined effects of temperature and GnHCl on structural and dynamical responses publication-title: ACS Omega – volume: 262 start-page: 470 year: 1984 end-page: 476 ident: bb0335 article-title: Studies on components 1’ (modified monomer) and 2 (dimer) formed during heat-treatment of bovine serum albumin publication-title: Colloid Polym. Sci. – volume: 211 start-page: 144 year: 2015 end-page: 162 ident: bb0070 article-title: The role of albumin receptors in regulation of albumin homeostasis: implications for drug delivery publication-title: J. Control. Release – volume: 110 start-page: 10540 year: 2006 end-page: 10549 ident: bb0135 article-title: Ultrafast solvation dynamics of human serum albumin: correlations with conformational transitions and site-selected recognition publication-title: J. Phys. Chem. B – volume: 40 start-page: 29 year: 2000 end-page: 38 ident: bb0205 article-title: Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation publication-title: Proteins – volume: 75 start-page: 1084 year: 1998 end-page: 1096 ident: bb0230 article-title: Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods publication-title: Biophys. J. – volume: 47 start-page: 7 year: 1984 end-page: 18 ident: bb0355 article-title: Thermal stability of human albumin measured by differential scanning calorimetry. I. Effects of caprylate and N-acetyltryptophanate publication-title: Vox Sang. – volume: 18 start-page: 11 year: 2019 ident: bb0200 article-title: Docetaxel-loaded human serum albumin (HSA) nanoparticles: synthesis, characterization, and evaluation publication-title: Biomed. Eng. Online – volume: 12 start-page: 439 year: 1999 end-page: 446 ident: bb0095 article-title: Crystal structure of human serum albumin at 2.5 Å resolution publication-title: Protein Eng. Des. Sel. – volume: 6 start-page: 495 year: 2016 end-page: 507 ident: bb0180 article-title: Overview of albumin and its purification methods publication-title: Adv. Pharm. Bull. – volume: 45 start-page: 1255 year: 1995 ident: bb0195 article-title: Thermal denaturation of bovine serum albumin and its oligomers and derivativespH dependence publication-title: J. Therm. Anal. – volume: 8 start-page: 33 year: 1976 end-page: 37 ident: bb0345 article-title: Heat denaturation of human serum albumin. Migration of bound fatty acids publication-title: Int. J. Pept. Protein Res. – volume: 1750 start-page: 93 year: 2005 end-page: 102 ident: bb0210 article-title: Guanidine hydrochloride denaturation of human serum albumin originates by local unfolding of some stable loops in domain III publication-title: Biochim. Biophys. Acta – volume: 85 start-page: 15 year: 1986 end-page: 22 ident: bb0190 article-title: Further evidence for the heterogeneity of serum albumin publication-title: Comp. Biochem. Physiol. B – volume: 118 start-page: 921 year: 2014 end-page: 930 ident: bb0140 article-title: Electrostatic unfolding and interactions of albumin driven by pH changes: a molecular dynamics study publication-title: J. Phys. Chem. B – volume: 104 start-page: 469 year: 1980 end-page: 478 ident: bb0215 article-title: Temperature behaviour of human serum albumin publication-title: Eur. J. Biochem. – volume: 123 start-page: 979 year: 2019 end-page: 990 ident: bb0080 article-title: Structure, enzymatic activities, glycation and therapeutic potential of human serum albumin: a natural cargo publication-title: Int. J. Biol. Macromol. – volume: 68 start-page: 459 year: 1946 end-page: 475 ident: bb0165 article-title: Preparation and properties of serum and plasma proteins. IV. A system for the separation into fractions of the protein and lipoprotein components of biological tissues and Fluids1a,b,c,d publication-title: J. Am. Chem. Soc. – volume: 263 start-page: 15392 year: 1988 end-page: 15399 ident: bb0365 article-title: Biphasic denaturation of human albumin due to ligand redistribution during unfolding publication-title: J. Biol. Chem. – volume: 358 start-page: 209 year: 1992 end-page: 215 ident: bb0090 article-title: Atomic structure and chemistry of human serum albumin publication-title: Nature – volume: 350 start-page: 277 year: 2006 end-page: 284 ident: bb0325 article-title: Differential scanning calorimetry as a tool to estimate binding parameters in multiligand binding proteins publication-title: Anal. Biochem. – volume: 46 start-page: 338 year: 1984 end-page: 340 ident: bb0170 article-title: Stabilization of serum albumin to heat, and inactivation of the hepatitis virus publication-title: Vox Sang. – volume: 26 start-page: 2229 year: 2017 end-page: 2239 ident: bb0390 article-title: Analysis of IgG kinetic stability by differential scanning calorimetry, probe fluorescence and light scattering publication-title: Protein Sci. – volume: 41 start-page: 705 year: 2016 end-page: 721 ident: bb0035 article-title: Investigation of the interaction between human serum albumin and two drugs as binary and ternary systems publication-title: Eur. J. Drug Metab. Pharmacokinet. – volume: 31 start-page: 1383 year: 1998 end-page: 1388 ident: bb0175 article-title: Purification of human albumin by the combination of the method of cohn with liquid chromatography publication-title: Braz. J. Med. Biol. Res. – volume: 22 start-page: 347 year: 1982 end-page: 351 ident: bb0185 article-title: Plasma derivatives and viral hepatitis publication-title: Transfusion – volume: 266 start-page: 26 year: 1999 end-page: 32 ident: bb0370 article-title: Molten globule-like state of human serum albumin at low pH publication-title: Eur. J. Biochem. – volume: 10 start-page: 607 year: 2018 end-page: 623 ident: bb0395 article-title: Modification of the kinetic stability of immunoglobulin G by solvent additives publication-title: MAbs – volume: 61 start-page: 921 year: 1992 end-page: 935 ident: bb0225 article-title: Theoretical analysis of lumry-eyring models in differential scanning calorimetry publication-title: Biophys. J. – volume: 105 start-page: 1572 year: 2017 end-page: 1580 ident: bb0310 article-title: Binding of erucic acid with human serum albumin using a spectroscopic and molecular docking study publication-title: Int. J. Biol. Macromol. – volume: 1830 year: 2013 ident: bb0060 article-title: Albumin as a versatile platform for drug half-life extension publication-title: Biochim. Biophys. Acta – volume: 75 start-page: 447 year: 2015 end-page: 452 ident: bb0235 article-title: Thermal induced unfolding of human serum albumin isomers: assigning residual α helices to domain II publication-title: Int. J. Biol. Macromol. – volume: 107 start-page: 2941 year: 2014 end-page: 2949 ident: bb0265 article-title: The kinetic stability of cytochrome c oxidase: effect of bound phospholipid and dimerization publication-title: Biophys. J. – volume: 88 start-page: 671 year: 2006 end-page: 679 ident: bb0020 article-title: The potential impact of tobacco biopharming: the case of human serum albumin publication-title: Am. J. Agric. Econ. – volume: 22 start-page: 77 year: 2010 end-page: 87 ident: bb0050 article-title: Ligand binding strategies of human serum albumin: how can the cargo be utilized? publication-title: Chirality – volume: 90 start-page: 187 year: 2008 end-page: 197 ident: bb0380 article-title: Resonance energy transfer and ligand binding studies on pH-induced folded states of human serum albumin publication-title: J. Photochem. Photobiol. B Biol. – volume: 221 start-page: 17 year: 2017 end-page: 25 ident: bb0255 article-title: Elucidation of μs dynamics of domain-III of human serum albumin during the chemical and thermal unfolding: a fluorescence correlation spectroscopic investigation publication-title: Biophys. Chem. – volume: 574 start-page: 189 year: 1979 end-page: 196 ident: bb0350 article-title: Thermal stability of fatty acid-serum albumin complexes studied by differential scanning calorimetry publication-title: Biochim. Biophys. Acta – volume: 12 start-page: 1972 year: 2016 end-page: 1988 ident: bb0155 article-title: Role of the protonation state on the structure and dynamics of albumin publication-title: J. Chem. Theory Comput. – volume: 20 start-page: 63 year: 1997 end-page: 73 ident: bb0220 article-title: Thermodynamic features of the thermal unfolding of human serum albumin publication-title: Int. J. Biol. Macromol. – volume: 5 start-page: 18218 year: 2015 end-page: 18232 ident: bb0150 article-title: Biophysical investigation of thymoquinone binding to ‘N’ and ‘B’ isoforms of human serum albumin: exploring the interaction mechanism and radical scavenging activity publication-title: RSC Adv. – volume: 123 start-page: 469 year: 2014 end-page: 477 ident: bb0145 article-title: Interaction of 5-fluoro-5′-deoxyuridine with human serum albumin under physiological and non-physiological condition: a biophysical investigation publication-title: Colloids Surf. B: Biointerfaces – volume: 39 start-page: 530 year: 2006 end-page: 536 ident: bb0240 article-title: Conformational study of human serum albumin in pre-denaturation temperatures by differential scanning calorimetry, circular dichroism and UV spectroscopy publication-title: BMB Rep. – volume: 47 start-page: 28 year: 1984 end-page: 40 ident: bb0360 article-title: Stabilization of human albumin by caprylate and acetyltryptophanate publication-title: Vox Sang. – volume: 33 start-page: 209 year: 2012 end-page: 290 ident: bb0010 article-title: Human serum albumin: from bench to bedside publication-title: Mol. Asp. Med. – year: 1996 ident: bb0385 article-title: All About Albumin: Biochemistry, Genetics and Medical Applications – volume: 8 start-page: 2094 year: 2018 end-page: 2106 ident: bb0065 article-title: Development of a novel albumin-based and maleimidopropionic acid-conjugated peptide with prolonged half-life and increased in vivo anti-tumor efficacy publication-title: Theranostics – volume: 258 start-page: 199 year: 1989 end-page: 204 ident: bb0160 article-title: Conformational changes in human serum albumin studied by fluorescence and absorption spectroscopy. Distance measurements as a function of pH and fatty acids publication-title: Biochem. J. – volume: 84 start-page: 113 year: 2006 end-page: 117 ident: bb0320 article-title: Comprative DSC study of human and bovin serum albumin publication-title: J. Therm. Anal. Calorim. – volume: 193 start-page: 948 year: 2021 end-page: 955 ident: bb0085 article-title: Review: roles of human serum albumin in prediction, diagnoses and treatment of COVID-19 publication-title: Int. J. Biol. Macromol. – volume: 20 start-page: 81 year: 2001 end-page: 89 ident: bb0315 article-title: The participation of human serum albumin domains in chemical and thermal unfolding publication-title: J. Protein Chem. – volume: 263 start-page: 11196 year: 1988 ident: 10.1016/j.ijbiomac.2023.123379_bb0340 article-title: Decrease in stability of human albumin with increase in protein concentration publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)37941-9 – volume: 22 start-page: 347 year: 1982 ident: 10.1016/j.ijbiomac.2023.123379_bb0185 article-title: Plasma derivatives and viral hepatitis publication-title: Transfusion doi: 10.1046/j.1537-2995.1982.22583017454.x – volume: 1830 start-page: 5394 year: 2013 ident: 10.1016/j.ijbiomac.2023.123379_bb0275 article-title: Binding, unfolding and refolding dynamics of serum albumins publication-title: Biochim. Biophys. Acta Gen. Subj. doi: 10.1016/j.bbagen.2013.05.017 – volume: 22 start-page: 77 year: 2010 ident: 10.1016/j.ijbiomac.2023.123379_bb0050 article-title: Ligand binding strategies of human serum albumin: how can the cargo be utilized? publication-title: Chirality doi: 10.1002/chir.20709 – volume: 3 start-page: 10406 year: 2018 ident: 10.1016/j.ijbiomac.2023.123379_bb0245 article-title: Region-specific double denaturation of human serum albumin: combined effects of temperature and GnHCl on structural and dynamical responses publication-title: ACS Omega doi: 10.1021/acsomega.8b00967 – volume: 221 start-page: 17 year: 2017 ident: 10.1016/j.ijbiomac.2023.123379_bb0255 article-title: Elucidation of μs dynamics of domain-III of human serum albumin during the chemical and thermal unfolding: a fluorescence correlation spectroscopic investigation publication-title: Biophys. Chem. doi: 10.1016/j.bpc.2016.11.006 – volume: 31 start-page: 1383 year: 1998 ident: 10.1016/j.ijbiomac.2023.123379_bb0175 article-title: Purification of human albumin by the combination of the method of cohn with liquid chromatography publication-title: Braz. J. Med. Biol. Res. doi: 10.1590/S0100-879X1998001100003 – volume: 107 start-page: 2941 year: 2014 ident: 10.1016/j.ijbiomac.2023.123379_bb0265 article-title: The kinetic stability of cytochrome c oxidase: effect of bound phospholipid and dimerization publication-title: Biophys. J. doi: 10.1016/j.bpj.2014.10.055 – volume: 20 start-page: 63 year: 1997 ident: 10.1016/j.ijbiomac.2023.123379_bb0220 article-title: Thermodynamic features of the thermal unfolding of human serum albumin publication-title: Int. J. Biol. Macromol. doi: 10.1016/S0141-8130(96)01153-1 – volume: 574 start-page: 189 year: 1979 ident: 10.1016/j.ijbiomac.2023.123379_bb0350 article-title: Thermal stability of fatty acid-serum albumin complexes studied by differential scanning calorimetry publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2760(79)90001-8 – volume: 15 start-page: 1445 year: 2018 ident: 10.1016/j.ijbiomac.2023.123379_bb0075 article-title: Binding of tolperisone hydrochloride with human serum albumin: effects on the conformation, thermodynamics, and activity of HSA publication-title: Mol. Pharm. doi: 10.1021/acs.molpharmaceut.7b00976 – year: 1996 ident: 10.1016/j.ijbiomac.2023.123379_bb0385 – volume: 18 start-page: 263 year: 1973 ident: 10.1016/j.ijbiomac.2023.123379_bb0375 article-title: Fluorescence and the location of tryptophan residues in protein molecules publication-title: Photochem. Photobiol. doi: 10.1111/j.1751-1097.1973.tb06422.x – volume: 358 start-page: 209 year: 1992 ident: 10.1016/j.ijbiomac.2023.123379_bb0090 article-title: Atomic structure and chemistry of human serum albumin publication-title: Nature doi: 10.1038/358209a0 – volume: 45 start-page: 1255 year: 1995 ident: 10.1016/j.ijbiomac.2023.123379_bb0195 article-title: Thermal denaturation of bovine serum albumin and its oligomers and derivativespH dependence publication-title: J. Therm. Anal. doi: 10.1007/BF02547420 – volume: 174 start-page: 37 year: 2017 ident: 10.1016/j.ijbiomac.2023.123379_bb0030 article-title: Negligible interaction of [Ru(Phen)3]2+ with human serum albumin makes it promising for a reliable in vivo assessment of the tissue oxygenation publication-title: J. Inorg. Biochem. doi: 10.1016/j.jinorgbio.2017.05.016 – volume: 350 start-page: 277 year: 2006 ident: 10.1016/j.ijbiomac.2023.123379_bb0325 article-title: Differential scanning calorimetry as a tool to estimate binding parameters in multiligand binding proteins publication-title: Anal. Biochem. doi: 10.1016/j.ab.2005.12.029 – volume: 88 start-page: 671 year: 2006 ident: 10.1016/j.ijbiomac.2023.123379_bb0020 article-title: The potential impact of tobacco biopharming: the case of human serum albumin publication-title: Am. J. Agric. Econ. doi: 10.1111/j.1467-8276.2006.00887.x – volume: 5 start-page: 18218 year: 2015 ident: 10.1016/j.ijbiomac.2023.123379_bb0150 article-title: Biophysical investigation of thymoquinone binding to ‘N’ and ‘B’ isoforms of human serum albumin: exploring the interaction mechanism and radical scavenging activity publication-title: RSC Adv. doi: 10.1039/C4RA09892G – volume: 10 start-page: 6741 year: 2008 ident: 10.1016/j.ijbiomac.2023.123379_bb0125 article-title: About the albumin structure in solution: cigar expanded form versus heart Normal shape publication-title: Phys. Chem. Chem. Phys. doi: 10.1039/b808938h – volume: 266 start-page: 26 year: 1999 ident: 10.1016/j.ijbiomac.2023.123379_bb0370 article-title: Molten globule-like state of human serum albumin at low pH publication-title: Eur. J. Biochem. doi: 10.1046/j.1432-1327.1999.00810.x – volume: 13 start-page: 3098 year: 2016 ident: 10.1016/j.ijbiomac.2023.123379_bb0025 article-title: Multidrug delivery systems based on human serum albumin for combination therapy with three anticancer agents publication-title: Mol. Pharm. doi: 10.1021/acs.molpharmaceut.6b00277 – volume: 12 start-page: 1972 year: 2016 ident: 10.1016/j.ijbiomac.2023.123379_bb0155 article-title: Role of the protonation state on the structure and dynamics of albumin publication-title: J. Chem. Theory Comput. doi: 10.1021/acs.jctc.5b01001 – volume: 15 start-page: 449 year: 1998 ident: 10.1016/j.ijbiomac.2023.123379_bb0250 article-title: Species differences of serum albumins: II. Chemical and thermal stability publication-title: Pharm. Res. doi: 10.1023/A:1011932516717 – volume: 263 start-page: 15392 year: 1988 ident: 10.1016/j.ijbiomac.2023.123379_bb0365 article-title: Biphasic denaturation of human albumin due to ligand redistribution during unfolding publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)37601-X – volume: 84 start-page: 113 year: 2006 ident: 10.1016/j.ijbiomac.2023.123379_bb0320 article-title: Comprative DSC study of human and bovin serum albumin publication-title: J. Therm. Anal. Calorim. doi: 10.1007/s10973-005-7170-1 – volume: 353 start-page: 38 year: 2005 ident: 10.1016/j.ijbiomac.2023.123379_bb0015 article-title: Structural basis of the drug-binding specificity of human serum albumin publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2005.07.075 – volume: 6 start-page: 116 year: 2016 ident: 10.1016/j.ijbiomac.2023.123379_bb0055 article-title: Human serum albumin nanoparticles for use in cancer drug delivery: process optimization and in vitro characterization publication-title: Nanomaterials (Basel) doi: 10.3390/nano6060116 – volume: 90 start-page: 187 year: 2008 ident: 10.1016/j.ijbiomac.2023.123379_bb0380 article-title: Resonance energy transfer and ligand binding studies on pH-induced folded states of human serum albumin publication-title: J. Photochem. Photobiol. B Biol. doi: 10.1016/j.jphotobiol.2008.01.001 – volume: 24 start-page: 1100 year: 2015 ident: 10.1016/j.ijbiomac.2023.123379_bb0260 article-title: Advanced analyses of kinetic stabilities of iggs modified by mutations and glycosylation publication-title: Protein Sci. doi: 10.1002/pro.2691 – volume: 303 start-page: 721 year: 2000 ident: 10.1016/j.ijbiomac.2023.123379_bb0100 article-title: Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2000.4158 – start-page: 53 year: 1977 ident: 10.1016/j.ijbiomac.2023.123379_bb0005 article-title: Some aspects of the structure and conformational properties of serum albumin – volume: 8 start-page: 33 year: 1976 ident: 10.1016/j.ijbiomac.2023.123379_bb0345 article-title: Heat denaturation of human serum albumin. Migration of bound fatty acids publication-title: Int. J. Pept. Protein Res. doi: 10.1111/j.1399-3011.1976.tb02478.x – volume: 5 start-page: 827 year: 1998 ident: 10.1016/j.ijbiomac.2023.123379_bb0115 article-title: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites publication-title: Nat. Struct. Biol. doi: 10.1038/1869 – volume: 30 start-page: 14894 year: 2014 ident: 10.1016/j.ijbiomac.2023.123379_bb0280 article-title: Concentration-dependent reversible self-oligomerization of serum albumins through intermolecular β-sheet formation publication-title: Langmuir doi: 10.1021/la5034959 – volume: 211 start-page: 144 year: 2015 ident: 10.1016/j.ijbiomac.2023.123379_bb0070 article-title: The role of albumin receptors in regulation of albumin homeostasis: implications for drug delivery publication-title: J. Control. Release doi: 10.1016/j.jconrel.2015.06.006 – volume: 13 start-page: 1825 year: 2022 ident: 10.1016/j.ijbiomac.2023.123379_bb0270 article-title: Human serum albumin dimerization enhances the S2 emission of bound cyanine IR806 publication-title: J. Phys. Chem. Lett. doi: 10.1021/acs.jpclett.1c03735 – volume: 11 start-page: 824 year: 1975 ident: 10.1016/j.ijbiomac.2023.123379_bb0045 article-title: The characterization of two specific drug binding sites on human serum albumin publication-title: Mol. Pharmacol. – volume: 41 start-page: 705 year: 2016 ident: 10.1016/j.ijbiomac.2023.123379_bb0035 article-title: Investigation of the interaction between human serum albumin and two drugs as binary and ternary systems publication-title: Eur. J. Drug Metab. Pharmacokinet. doi: 10.1007/s13318-015-0297-y – volume: 314 start-page: 955 year: 2001 ident: 10.1016/j.ijbiomac.2023.123379_bb0105 article-title: Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2000.5208 – volume: 118 start-page: 921 year: 2014 ident: 10.1016/j.ijbiomac.2023.123379_bb0140 article-title: Electrostatic unfolding and interactions of albumin driven by pH changes: a molecular dynamics study publication-title: J. Phys. Chem. B doi: 10.1021/jp409936v – volume: 105 start-page: 1572 year: 2017 ident: 10.1016/j.ijbiomac.2023.123379_bb0310 article-title: Binding of erucic acid with human serum albumin using a spectroscopic and molecular docking study publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2017.04.051 – volume: 1441 start-page: 131 year: 1999 ident: 10.1016/j.ijbiomac.2023.123379_bb0120 article-title: Fatty acid binding to human serum albumin: new insights from crystallographic studies publication-title: Biochim. Biophys. Acta doi: 10.1016/S1388-1981(99)00148-1 – volume: 47 start-page: 7 year: 1984 ident: 10.1016/j.ijbiomac.2023.123379_bb0355 article-title: Thermal stability of human albumin measured by differential scanning calorimetry. I. Effects of caprylate and N-acetyltryptophanate publication-title: Vox Sang. – volume: 40 start-page: 29 year: 2000 ident: 10.1016/j.ijbiomac.2023.123379_bb0205 article-title: Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation publication-title: Proteins doi: 10.1002/(SICI)1097-0134(20000701)40:1<29::AID-PROT50>3.0.CO;2-P – volume: 1750 start-page: 93 year: 2005 ident: 10.1016/j.ijbiomac.2023.123379_bb0210 article-title: Guanidine hydrochloride denaturation of human serum albumin originates by local unfolding of some stable loops in domain III publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbapap.2005.04.001 – volume: 75 start-page: 447 year: 2015 ident: 10.1016/j.ijbiomac.2023.123379_bb0235 article-title: Thermal induced unfolding of human serum albumin isomers: assigning residual α helices to domain II publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2015.02.003 – volume: 104 start-page: 469 year: 1980 ident: 10.1016/j.ijbiomac.2023.123379_bb0215 article-title: Temperature behaviour of human serum albumin publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1980.tb04449.x – volume: 14 start-page: 1656 year: 2017 ident: 10.1016/j.ijbiomac.2023.123379_bb0305 article-title: Biophysical study on the interaction between eperisone hydrochloride and human serum albumin using spectroscopic, calorimetric, and molecular docking analyses publication-title: Mol. Pharm. doi: 10.1021/acs.molpharmaceut.6b01124 – volume: 68 start-page: 459 year: 1946 ident: 10.1016/j.ijbiomac.2023.123379_bb0165 article-title: Preparation and properties of serum and plasma proteins. IV. A system for the separation into fractions of the protein and lipoprotein components of biological tissues and Fluids1a,b,c,d publication-title: J. Am. Chem. Soc. doi: 10.1021/ja01207a034 – volume: 258 start-page: 199 year: 1989 ident: 10.1016/j.ijbiomac.2023.123379_bb0160 article-title: Conformational changes in human serum albumin studied by fluorescence and absorption spectroscopy. Distance measurements as a function of pH and fatty acids publication-title: Biochem. J. doi: 10.1042/bj2580199 – volume: 26 start-page: 2229 year: 2017 ident: 10.1016/j.ijbiomac.2023.123379_bb0390 article-title: Analysis of IgG kinetic stability by differential scanning calorimetry, probe fluorescence and light scattering publication-title: Protein Sci. doi: 10.1002/pro.3278 – volume: 12 start-page: 439 year: 1999 ident: 10.1016/j.ijbiomac.2023.123379_bb0095 article-title: Crystal structure of human serum albumin at 2.5 Å resolution publication-title: Protein Eng. Des. Sel. doi: 10.1093/protein/12.6.439 – volume: 3 start-page: 485 year: 2004 ident: 10.1016/j.ijbiomac.2023.123379_bb0300 article-title: Use of the phase diagram method to analyze the protein unfolding-refolding reactions: fishing out the “invisible” intermediates publication-title: J. Proteome Res. doi: 10.1021/pr034094y – volume: 46 start-page: 338 year: 1984 ident: 10.1016/j.ijbiomac.2023.123379_bb0170 article-title: Stabilization of serum albumin to heat, and inactivation of the hepatitis virus publication-title: Vox Sang. doi: 10.1111/j.1423-0410.1984.tb00096.x – volume: 20 start-page: 81 year: 2001 ident: 10.1016/j.ijbiomac.2023.123379_bb0315 article-title: The participation of human serum albumin domains in chemical and thermal unfolding publication-title: J. Protein Chem. doi: 10.1023/A:1011000317042 – volume: 18 start-page: 11 year: 2019 ident: 10.1016/j.ijbiomac.2023.123379_bb0200 article-title: Docetaxel-loaded human serum albumin (HSA) nanoparticles: synthesis, characterization, and evaluation publication-title: Biomed. Eng. Online doi: 10.1186/s12938-019-0624-7 – volume: 2 start-page: 813 year: 2001 ident: 10.1016/j.ijbiomac.2023.123379_bb0290 article-title: Partially folded conformations in the folding pathway of bovine carbonic anhydrase II: a fluorescence spectroscopic analysis publication-title: Chembiochem doi: 10.1002/1439-7633(20011105)2:11<813::AID-CBIC813>3.0.CO;2-W – volume: 1830 year: 2013 ident: 10.1016/j.ijbiomac.2023.123379_bb0060 article-title: Albumin as a versatile platform for drug half-life extension publication-title: Biochim. Biophys. Acta – volume: 105 start-page: 19258 year: 2008 ident: 10.1016/j.ijbiomac.2023.123379_bb0330 article-title: In vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0806431105 – volume: 123 start-page: 979 year: 2019 ident: 10.1016/j.ijbiomac.2023.123379_bb0080 article-title: Structure, enzymatic activities, glycation and therapeutic potential of human serum albumin: a natural cargo publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2018.11.053 – volume: 262 start-page: 470 year: 1984 ident: 10.1016/j.ijbiomac.2023.123379_bb0335 article-title: Studies on components 1’ (modified monomer) and 2 (dimer) formed during heat-treatment of bovine serum albumin publication-title: Colloid Polym. Sci. doi: 10.1007/BF01412043 – volume: 33 start-page: 209 year: 2012 ident: 10.1016/j.ijbiomac.2023.123379_bb0010 article-title: Human serum albumin: from bench to bedside publication-title: Mol. Asp. Med. doi: 10.1016/j.mam.2011.12.002 – volume: 75 start-page: 1084 year: 1998 ident: 10.1016/j.ijbiomac.2023.123379_bb0230 article-title: Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods publication-title: Biophys. J. doi: 10.1016/S0006-3495(98)77598-8 – volume: 47 start-page: 28 year: 1984 ident: 10.1016/j.ijbiomac.2023.123379_bb0360 article-title: Stabilization of human albumin by caprylate and acetyltryptophanate publication-title: Vox Sang. doi: 10.1111/j.1423-0410.1984.tb01558.x – volume: 6 start-page: 495 year: 2016 ident: 10.1016/j.ijbiomac.2023.123379_bb0180 article-title: Overview of albumin and its purification methods publication-title: Adv. Pharm. Bull. doi: 10.15171/apb.2016.063 – volume: 85 start-page: 15 year: 1986 ident: 10.1016/j.ijbiomac.2023.123379_bb0190 article-title: Further evidence for the heterogeneity of serum albumin publication-title: Comp. Biochem. Physiol. B doi: 10.1016/0305-0491(86)90215-4 – volume: 1596 start-page: 138 year: 2002 ident: 10.1016/j.ijbiomac.2023.123379_bb0295 article-title: Unraveling multistate unfolding of rabbit muscle creatine kinase publication-title: Biochim. Biophys. Acta doi: 10.1016/S0167-4838(02)00212-1 – volume: 39 start-page: 530 year: 2006 ident: 10.1016/j.ijbiomac.2023.123379_bb0240 article-title: Conformational study of human serum albumin in pre-denaturation temperatures by differential scanning calorimetry, circular dichroism and UV spectroscopy publication-title: BMB Rep. doi: 10.5483/BMBRep.2006.39.5.530 – volume: 275 start-page: 3042 year: 2000 ident: 10.1016/j.ijbiomac.2023.123379_bb0130 article-title: Conformational transitions of the three recombinant domains of human serum albumin depending on pH publication-title: J. Biol. Chem. doi: 10.1074/jbc.275.5.3042 – volume: 356 year: 2022 ident: 10.1016/j.ijbiomac.2023.123379_bb0040 article-title: Novel perspective into the interaction behavior study of the cyanidin with human serum albumin-holo transferrin complex: spectroscopic, calorimetric and molecular modeling approaches publication-title: J. Mol. Liq. doi: 10.1016/j.molliq.2022.119042 – volume: 193 start-page: 948 year: 2021 ident: 10.1016/j.ijbiomac.2023.123379_bb0085 article-title: Review: roles of human serum albumin in prediction, diagnoses and treatment of COVID-19 publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2021.10.095 – volume: 148 start-page: 16 year: 2010 ident: 10.1016/j.ijbiomac.2023.123379_bb0110 article-title: Allostery in a monomeric protein: the case of human serum albumin publication-title: Biophys. Chem. doi: 10.1016/j.bpc.2010.03.001 – volume: 61 start-page: 921 year: 1992 ident: 10.1016/j.ijbiomac.2023.123379_bb0225 article-title: Theoretical analysis of lumry-eyring models in differential scanning calorimetry publication-title: Biophys. J. doi: 10.1016/S0006-3495(92)81899-4 – volume: 110 start-page: 10540 year: 2006 ident: 10.1016/j.ijbiomac.2023.123379_bb0135 article-title: Ultrafast solvation dynamics of human serum albumin: correlations with conformational transitions and site-selected recognition publication-title: J. Phys. Chem. B doi: 10.1021/jp055989w – volume: 10 start-page: 607 year: 2018 ident: 10.1016/j.ijbiomac.2023.123379_bb0395 article-title: Modification of the kinetic stability of immunoglobulin G by solvent additives publication-title: MAbs doi: 10.1080/19420862.2018.1450126 – volume: 123 start-page: 469 year: 2014 ident: 10.1016/j.ijbiomac.2023.123379_bb0145 article-title: Interaction of 5-fluoro-5′-deoxyuridine with human serum albumin under physiological and non-physiological condition: a biophysical investigation publication-title: Colloids Surf. B: Biointerfaces doi: 10.1016/j.colsurfb.2014.09.044 – volume: 8 start-page: 2094 year: 2018 ident: 10.1016/j.ijbiomac.2023.123379_bb0065 article-title: Development of a novel albumin-based and maleimidopropionic acid-conjugated peptide with prolonged half-life and increased in vivo anti-tumor efficacy publication-title: Theranostics doi: 10.7150/thno.22069 – volume: 26 start-page: 108 year: 2021 ident: 10.1016/j.ijbiomac.2023.123379_bb0285 article-title: Reversible dimerization of human serum albumin publication-title: Molecules doi: 10.3390/molecules26010108 |
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| SubjectTerms | calorimetry Calorimetry, Differential Scanning denaturation human serum albumin Humans Lumry-Eyring model Phase diagram method Protein Denaturation Protein thermal stability Serum albumin Serum Albumin, Human spectroscopy thermal stability Thermodynamic and kinetic stability Thermodynamics |
| Title | Explanation of inconsistencies in the determination of human serum albumin thermal stability |
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