Selective Recognition of Myoglobin in Biological Samples Using Molecularly Imprinted Polymer-Based Affinity Traps
The current work demonstrates the design, characterization, and preparation of molecularly imprinted microspheres for the selective detection of myoglobin in serum samples. The suspension polymerization approach was applied for the preparation of myoglobin imprinted microspheres. For this purpose, N...
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Published in | International journal of analytical chemistry Vol. 2018; no. 2018; pp. 1 - 9 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
Cairo, Egypt
Hindawi Publishing Corporation
01.01.2018
Hindawi John Wiley & Sons, Inc Hindawi Limited |
Subjects | |
Online Access | Get full text |
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Abstract | The current work demonstrates the design, characterization, and preparation of molecularly imprinted microspheres for the selective detection of myoglobin in serum samples. The suspension polymerization approach was applied for the preparation of myoglobin imprinted microspheres. For this purpose, N-methacryloylamino folic acid-Nd3+ (MAFol- Nd3+) was chosen as the complex functional monomer. The optimization studies were performed changing the medium pH, temperature, and myoglobin concentration. pH 7.0 was determined as the optimum value where the prepared imprinted microspheres displayed maximum binding for myoglobin. The maximum binding capacity was achieved as 623 mgg−1. In addition, the selectivity studies were conducted. The results confirmed that the imprinted microspheres showed great selectivity towards myoglobin in the existence of hemoglobin, cytochrome c, and lysozyme which were chosen as potentially competing proteins. |
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AbstractList | The current work demonstrates the design, characterization, and preparation of molecularly imprinted microspheres for the selective detection of myoglobin in serum samples. The suspension polymerization approach was applied for the preparation of myoglobin imprinted microspheres. For this purpose, N-methacryloylamino folic acid-Nd
3+
(MAFol- Nd
3+
) was chosen as the complex functional monomer. The optimization studies were performed changing the medium pH, temperature, and myoglobin concentration. pH 7.0 was determined as the optimum value where the prepared imprinted microspheres displayed maximum binding for myoglobin. The maximum binding capacity was achieved as 623 mgg
−1
. In addition, the selectivity studies were conducted. The results confirmed that the imprinted microspheres showed great selectivity towards myoglobin in the existence of hemoglobin, cytochrome c, and lysozyme which were chosen as potentially competing proteins. The current work demonstrates the design, characterization, and preparation of molecularly imprinted microspheres for the selective detection of myoglobin in serum samples. The suspension polymerization approach was applied for the preparation of myoglobin imprinted microspheres. For this purpose, N-methacryloylamino folic acid-Nd3+ (MAFol- Nd3+) was chosen as the complex functional monomer. The optimization studies were performed changing the medium pH, temperature, and myoglobin concentration. pH 7.0 was determined as the optimum value where the prepared imprinted microspheres displayed maximum binding for myoglobin. The maximum binding capacity was achieved as 623 mgg−1. In addition, the selectivity studies were conducted. The results confirmed that the imprinted microspheres showed great selectivity towards myoglobin in the existence of hemoglobin, cytochrome c, and lysozyme which were chosen as potentially competing proteins. The current work demonstrates the design, characterization, and preparation of molecularly imprinted microspheres for the selective detection of myoglobin in serum samples. The suspension polymerization approach was applied for the preparation of myoglobin imprinted microspheres. For this purpose, N-methacryloylamino folic acid-Nd (MAFol- Nd ) was chosen as the complex functional monomer. The optimization studies were performed changing the medium pH, temperature, and myoglobin concentration. pH 7.0 was determined as the optimum value where the prepared imprinted microspheres displayed maximum binding for myoglobin. The maximum binding capacity was achieved as 623 mgg . In addition, the selectivity studies were conducted. The results confirmed that the imprinted microspheres showed great selectivity towards myoglobin in the existence of hemoglobin, cytochrome c, and lysozyme which were chosen as potentially competing proteins. The current work demonstrates the design, characterization, and preparation of molecularly imprinted microspheres for the selective detection of myoglobin in serum samples. The suspension polymerization approach was applied for the preparation of myoglobin imprinted microspheres. For this purpose, N-methacryloylamino folic acid-[Nd.sup.3+] (MAFol- [Nd.sup.3+]) was chosen as the complex functional monomer. The optimization studies were performed changing the medium pH, temperature, and myoglobin concentration. pH 7.0 was determined as the optimum value where the prepared imprinted microspheres displayed maximum binding for myoglobin. The maximum binding capacity was achieved as 623 mg[g.sup.-1]. In addition, the selectivity studies were conducted. The results confirmed that the imprinted microspheres showed great selectivity towards myoglobin in the existence of hemoglobin, cytochrome c, and lysozyme which were chosen as potentially competing proteins. |
Audience | Academic |
Author | Keçili, Rüstem |
AuthorAffiliation | Anadolu University, Yunus Emre Vocational School of Health Services, Department of Medical Services and Techniques, 26470 Eskisehir, Turkey |
AuthorAffiliation_xml | – name: Anadolu University, Yunus Emre Vocational School of Health Services, Department of Medical Services and Techniques, 26470 Eskisehir, Turkey |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30174693$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_1016_j_trac_2023_117205 crossref_primary_10_3390_molecules26144252 crossref_primary_10_1021_acsomega_1c05554 crossref_primary_10_1080_01496395_2020_1869259 crossref_primary_10_1016_j_procbio_2019_09_032 crossref_primary_10_1016_j_saa_2019_117714 crossref_primary_10_1016_j_teac_2023_e00213 crossref_primary_10_1016_j_trac_2021_116431 |
Cites_doi | 10.1021/ac0491612 10.1021/ac061089f 10.1016/j.bios.2006.11.015 10.1016/j.bios.2013.02.012 10.1016/j.chroma.2018.05.038 10.3390/ijms12095908 10.1111/j.1365-2621.1994.tb14695.x 10.1016/j.bios.2011.01.001 10.1016/j.bioelechem.2012.07.006 10.1021/ja02242a004 10.1016/S0733-8627(05)70186-3 10.1039/c3tb20409j 10.1016/S0021-9673(01)91649-8 10.4037/ajcc1998.7.6.418 10.1016/S0196-0644(00)70129-6 10.1002/jssc.201200784 10.3390/s17030454 10.1016/0009-8981(92)90168-P 10.1016/j.actbio.2011.11.005 10.1002/chir.22273 10.1146/annurev.med.45.1.31 10.1021/pr050344u 10.1021/acs.iecr.5b00212 10.1021/ed086p600 10.47102/annals-acadmedsg.V39N3p210 10.1681/ASN.V771066 10.1002/mabi.200800273 10.1007/s11051-010-9962-x 10.1007/s12010-014-0844-z 10.1016/j.amjcard.2004.06.019 10.1016/j.electacta.2013.06.061 10.1016/0022-1759(85)90057-2 10.1093/ajcp/104.4.472 10.1016/j.polymer.2012.03.021 10.1039/C6PY01853J 10.1016/j.molstruc.2018.03.126 10.1016/j.aca.2012.10.053 10.4037/ccn1999.19.1.58 10.1016/j.bios.2017.08.058 |
ContentType | Journal Article |
Copyright | Copyright © 2018 Rüstem Keçili. COPYRIGHT 2018 John Wiley & Sons, Inc. Copyright © 2018 Rüstem Keçili. This is an open access article distributed under the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. https://creativecommons.org/licenses/by/4.0 Copyright © 2018 Rüstem Keçili. 2018 |
Copyright_xml | – notice: Copyright © 2018 Rüstem Keçili. – notice: COPYRIGHT 2018 John Wiley & Sons, Inc. – notice: Copyright © 2018 Rüstem Keçili. This is an open access article distributed under the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. https://creativecommons.org/licenses/by/4.0 – notice: Copyright © 2018 Rüstem Keçili. 2018 |
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SubjectTerms | Alcohol Analytical chemistry Binding Biological properties Book publishing Chromatography Cytochromes Folic acid Heart attacks Hemoglobin Lysozyme Microspheres Molecular imprinting Myoglobin Myoglobins Polymer industry Polymerization Polymers Proteins Selectivity Sensors Suspension polymerization Vitamin B |
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Title | Selective Recognition of Myoglobin in Biological Samples Using Molecularly Imprinted Polymer-Based Affinity Traps |
URI | https://search.emarefa.net/detail/BIM-1166379 https://dx.doi.org/10.1155/2018/4359892 https://www.ncbi.nlm.nih.gov/pubmed/30174693 https://www.proquest.com/docview/2090434465 https://search.proquest.com/docview/2099040413 https://pubmed.ncbi.nlm.nih.gov/PMC6106809 https://doaj.org/article/2327c033ac6b48deb3c432caca6a5f05 |
Volume | 2018 |
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