Effect of Trehalose and Ceftriaxone on the Stability of Aggregating-Prone Tau Peptide Containing PHF6 Sequence: An SRCD Study
The tau protein, a soluble protein associated with microtubules, which is involved in the assembly and stabilization of cytoskeletal elements, was found to form neurofibrillary tangles in different neurodegenerative diseases. Insoluble tau aggregates were observed to be organized in paired helical f...
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Published in | International journal of molecular sciences Vol. 23; no. 6; p. 2932 |
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Language | English |
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Abstract | The tau protein, a soluble protein associated with microtubules, which is involved in the assembly and stabilization of cytoskeletal elements, was found to form neurofibrillary tangles in different neurodegenerative diseases. Insoluble tau aggregates were observed to be organized in paired helical filaments (PHFs) and straight filaments (SFs). Recently, two small sequences (306-311 and 275-280) in the microtubule-binding region (MTBR), named PHF6 and PHF6*, respectively, were found to be essential for tau aggregation. Since a possible therapeutic approach consists of impairing amyloid formation either by stabilizing the native proteins or reducing the level of amyloid precursors, here we use synchrotron radiation circular dichroism (SRCD) at Diamond B23 beamline to evaluate the inhibitory effects of two small molecules, trehalose and ceftriaxone, against the aggregation of a small peptide containing the PHF6* sequence. Our results indicate that both these molecules, ceftriaxone and trehalose, increased the stability of the peptide toward aggregation, in particular that induced by heparin. With trehalose being present in many fruits, vegetables, algae and processed foods, these results support the need to investigate whether a diet richer in trehalose might exert a protective effect toward pathologies linked to protein misfolding. |
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AbstractList | The tau protein, a soluble protein associated with microtubules, which is involved in the assembly and stabilization of cytoskeletal elements, was found to form neurofibrillary tangles in different neurodegenerative diseases. Insoluble tau aggregates were observed to be organized in paired helical filaments (PHFs) and straight filaments (SFs). Recently, two small sequences (306–311 and 275–280) in the microtubule-binding region (MTBR), named PHF6 and PHF6*, respectively, were found to be essential for tau aggregation. Since a possible therapeutic approach consists of impairing amyloid formation either by stabilizing the native proteins or reducing the level of amyloid precursors, here we use synchrotron radiation circular dichroism (SRCD) at Diamond B23 beamline to evaluate the inhibitory effects of two small molecules, trehalose and ceftriaxone, against the aggregation of a small peptide containing the PHF6* sequence. Our results indicate that both these molecules, ceftriaxone and trehalose, increased the stability of the peptide toward aggregation, in particular that induced by heparin. With trehalose being present in many fruits, vegetables, algae and processed foods, these results support the need to investigate whether a diet richer in trehalose might exert a protective effect toward pathologies linked to protein misfolding. The tau protein, a soluble protein associated with microtubules, which is involved in the assembly and stabilization of cytoskeletal elements, was found to form neurofibrillary tangles in different neurodegenerative diseases. Insoluble tau aggregates were observed to be organized in paired helical filaments (PHFs) and straight filaments (SFs). Recently, two small sequences (306-311 and 275-280) in the microtubule-binding region (MTBR), named PHF6 and PHF6*, respectively, were found to be essential for tau aggregation. Since a possible therapeutic approach consists of impairing amyloid formation either by stabilizing the native proteins or reducing the level of amyloid precursors, here we use synchrotron radiation circular dichroism (SRCD) at Diamond B23 beamline to evaluate the inhibitory effects of two small molecules, trehalose and ceftriaxone, against the aggregation of a small peptide containing the PHF6* sequence. Our results indicate that both these molecules, ceftriaxone and trehalose, increased the stability of the peptide toward aggregation, in particular that induced by heparin. With trehalose being present in many fruits, vegetables, algae and processed foods, these results support the need to investigate whether a diet richer in trehalose might exert a protective effect toward pathologies linked to protein misfolding.The tau protein, a soluble protein associated with microtubules, which is involved in the assembly and stabilization of cytoskeletal elements, was found to form neurofibrillary tangles in different neurodegenerative diseases. Insoluble tau aggregates were observed to be organized in paired helical filaments (PHFs) and straight filaments (SFs). Recently, two small sequences (306-311 and 275-280) in the microtubule-binding region (MTBR), named PHF6 and PHF6*, respectively, were found to be essential for tau aggregation. Since a possible therapeutic approach consists of impairing amyloid formation either by stabilizing the native proteins or reducing the level of amyloid precursors, here we use synchrotron radiation circular dichroism (SRCD) at Diamond B23 beamline to evaluate the inhibitory effects of two small molecules, trehalose and ceftriaxone, against the aggregation of a small peptide containing the PHF6* sequence. Our results indicate that both these molecules, ceftriaxone and trehalose, increased the stability of the peptide toward aggregation, in particular that induced by heparin. With trehalose being present in many fruits, vegetables, algae and processed foods, these results support the need to investigate whether a diet richer in trehalose might exert a protective effect toward pathologies linked to protein misfolding. |
Author | Torni, Federica Ruzza, Paolo Hussain, Rohanah Siligardi, Giuliano Honisch, Claudia |
AuthorAffiliation | 2 Department of Chemical Sciences, University of Padua, Via Marzolo 1, 35131 Padova, Italy 1 Institute of Biomolecular Chemistry of CNR, Padua Unit, Via Marzolo 1, 35131 Padova, Italy; c.honisch@icb.cnr.it (C.H.); tornifederica@gmail.com (F.T.) 3 Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK; rohanah.hussain@diamond.ac.uk |
AuthorAffiliation_xml | – name: 3 Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK; rohanah.hussain@diamond.ac.uk – name: 2 Department of Chemical Sciences, University of Padua, Via Marzolo 1, 35131 Padova, Italy – name: 1 Institute of Biomolecular Chemistry of CNR, Padua Unit, Via Marzolo 1, 35131 Padova, Italy; c.honisch@icb.cnr.it (C.H.); tornifederica@gmail.com (F.T.) |
Author_xml | – sequence: 1 givenname: Claudia orcidid: 0000-0001-9720-6176 surname: Honisch fullname: Honisch, Claudia organization: Department of Chemical Sciences, University of Padua, Via Marzolo 1, 35131 Padova, Italy – sequence: 2 givenname: Federica surname: Torni fullname: Torni, Federica organization: Institute of Biomolecular Chemistry of CNR, Padua Unit, Via Marzolo 1, 35131 Padova, Italy – sequence: 3 givenname: Rohanah orcidid: 0000-0001-6207-6631 surname: Hussain fullname: Hussain, Rohanah organization: Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK – sequence: 4 givenname: Paolo orcidid: 0000-0002-5596-9295 surname: Ruzza fullname: Ruzza, Paolo organization: Institute of Biomolecular Chemistry of CNR, Padua Unit, Via Marzolo 1, 35131 Padova, Italy – sequence: 5 givenname: Giuliano orcidid: 0000-0002-4667-6423 surname: Siligardi fullname: Siligardi, Giuliano organization: Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK |
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Cites_doi | 10.3390/biom11020333 10.1016/j.pnpbp.2009.11.021 10.1016/j.bpc.2021.106694 10.1016/j.bbagen.2018.02.014 10.1021/cn200072h 10.1002/chir.23210 10.1107/S1600577515007602 10.1007/978-1-61779-927-3_22 10.1039/C5SM01896J 10.4103/1673-5374.274329 10.1016/j.bbagen.2016.04.021 10.3390/biom5020724 10.1021/bi061422+ 10.1039/D1RA05397C 10.1021/acs.jpcb.6b07045 10.1039/c3cp00063j 10.3389/fnins.2021.643115 10.1074/jbc.M105196200 10.1073/pnas.1418155112 10.1007/s00401-017-1707-9 10.1073/pnas.1500851112 10.1002/pro.3 10.1074/jbc.M501565200 10.1021/bi2010569 10.1007/s00726-013-1503-3 10.1073/pnas.1301440110 10.1021/cn400149k 10.1021/acsomega.0c05638 10.3390/molecules25051195 10.1093/jnen/nlaa016 10.1093/nar/gky497 10.1016/j.tips.2017.03.011 10.1007/s10571-006-9083-3 10.1111/j.1750-3639.2007.00053.x |
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Keywords | ceftriaxone synchrotron radiation circular dichroism protein aggregation conformational stability tauopathies trehalose transmission electron microscopy intrinsically disordered proteins tau protein |
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References | Guo (ref_3) 2017; 133 Hussain (ref_34) 2015; 22 Chen (ref_31) 2021; 11 Micsonai (ref_33) 2015; 112 Mamun (ref_5) 2020; 15 Honisch (ref_20) 2020; 32 Sechi (ref_25) 2010; 34 Ruzza (ref_24) 2016; 1860 Jain (ref_27) 2009; 18 Skrabana (ref_6) 2006; 26 Luyckx (ref_28) 2011; 5 Behrendt (ref_37) 2016; 22 Chemes (ref_30) 2012; 895 Mandelkow (ref_35) 2007; 17 Levine (ref_14) 2015; 112 Ordiales (ref_16) 2020; 79 Holmes (ref_17) 2013; 110 Ahanger (ref_36) 2021; 6 Micsonai (ref_32) 2018; 46 Li (ref_11) 2006; 45 Marchiani (ref_19) 2013; 45 Smit (ref_10) 2017; 121 Larini (ref_15) 2013; 15 Uversky (ref_1) 2021; 279 Barghorn (ref_13) 2001; 276 (ref_18) 2017; Volume 7 Bachmann (ref_9) 2021; 15 Combs (ref_12) 2011; 50 ref_2 Ruzza (ref_21) 2015; 5 Ruzza (ref_23) 2018; 1862 Ruzza (ref_22) 2014; 5 Orr (ref_4) 2017; 38 Leung (ref_26) 2012; 3 Siddhanta (ref_29) 2015; 11 ref_7 Mukrasch (ref_8) 2005; 280 |
References_xml | – ident: ref_2 doi: 10.3390/biom11020333 – volume: 34 start-page: 416 year: 2010 ident: ref_25 article-title: Ceftriaxone has a therapeutic role in Alexander disease publication-title: Prog. Neuro-Psychopharmacol. Biol. Psychiatry doi: 10.1016/j.pnpbp.2009.11.021 contributor: fullname: Sechi – volume: 22 start-page: 4 year: 2016 ident: ref_37 article-title: Advances in Fmoc solid-phase peptide synthesis publication-title: J. Pept. Sci. Off. Publ. Eur. Pept. Soc. contributor: fullname: Behrendt – volume: 279 start-page: 106694 year: 2021 ident: ref_1 article-title: Intrinsically disordered proteins: Chronology of a discovery publication-title: Biophys. Chem. doi: 10.1016/j.bpc.2021.106694 contributor: fullname: Uversky – volume: 1862 start-page: 1317 year: 2018 ident: ref_23 article-title: Chaperone-like effect of ceftriaxone on HEWL aggregation: A spectroscopic and computational study publication-title: Biochim. Biophys. Acta Gen. Sub. doi: 10.1016/j.bbagen.2018.02.014 contributor: fullname: Ruzza – volume: 3 start-page: 22 year: 2012 ident: ref_26 article-title: Ceftriaxone Ameliorates Motor Deficits and Protects Dopaminergic Neurons in 6-Hydroxydopamine-Lesioned Rats publication-title: ACS Chem. Neurosci. doi: 10.1021/cn200072h contributor: fullname: Leung – volume: Volume 7 start-page: 3 year: 2017 ident: ref_18 article-title: Small Molecules that Ameliorate Protein Misfolding publication-title: Advances in Organic Synthesis – volume: 32 start-page: 611 year: 2020 ident: ref_20 article-title: Influence of small molecules on the photo-stability of water soluble porcine lens proteins publication-title: Chirality doi: 10.1002/chir.23210 contributor: fullname: Honisch – volume: 22 start-page: 862 year: 2015 ident: ref_34 article-title: CDApps: Integrated software for experimental planning and data processing at beamline B23, Diamond Light Source publication-title: J. Synchrotron Radiat. doi: 10.1107/S1600577515007602 contributor: fullname: Hussain – volume: 895 start-page: 387 year: 2012 ident: ref_30 article-title: Circular dichroism techniques for the analysis of intrinsically disordered proteins and domains publication-title: Methods Mol. Biol. doi: 10.1007/978-1-61779-927-3_22 contributor: fullname: Chemes – volume: 11 start-page: 7241 year: 2015 ident: ref_29 article-title: Revealing the trehalose mediated inhibition of protein aggregation through lysozyme-silver nanoparticle interaction publication-title: Soft Matter doi: 10.1039/C5SM01896J contributor: fullname: Siddhanta – volume: 15 start-page: 1417 year: 2020 ident: ref_5 article-title: Toxic tau: Structural origins of tau aggregation in Alzheimer’s disease publication-title: Neural Regen. Res. doi: 10.4103/1673-5374.274329 contributor: fullname: Mamun – volume: 1860 start-page: 2239 year: 2016 ident: ref_24 article-title: Interactions of GFAP with ceftriaxone and phenytoin: SRCD and molecular docking and dynamic simulation publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbagen.2016.04.021 contributor: fullname: Ruzza – volume: 5 start-page: 724 year: 2015 ident: ref_21 article-title: Effects of Trehalose on Thermodynamic Properties of Alpha-synuclein Revealed through Synchrotron Radiation Circular Dichroism publication-title: Biomolecules doi: 10.3390/biom5020724 contributor: fullname: Ruzza – volume: 45 start-page: 15692 year: 2006 ident: ref_11 article-title: Characterization of Two VQIXXK Motifs for Tau Fibrillization in Vitro publication-title: Biochemistry doi: 10.1021/bi061422+ contributor: fullname: Li – volume: 11 start-page: 37290 year: 2021 ident: ref_31 article-title: Oligomeric procyanidins inhibit insulin fibrillation by forming unstructured and off-pathway aggregates publication-title: RSC Adv. doi: 10.1039/D1RA05397C contributor: fullname: Chen – volume: 121 start-page: 3250 year: 2017 ident: ref_10 article-title: Primary Fibril Nucleation of Aggregation Prone Tau Fragments PHF6 and PHF6* publication-title: J. Phys. Chem. B doi: 10.1021/acs.jpcb.6b07045 contributor: fullname: Smit – volume: 15 start-page: 8916 year: 2013 ident: ref_15 article-title: Initiation of assembly of tau (273–284) and its ΔK280 mutant: An experimental and computational study publication-title: Phys. Chem. Chem. Phys. doi: 10.1039/c3cp00063j contributor: fullname: Larini – volume: 15 start-page: 547 year: 2021 ident: ref_9 article-title: Differential Effects of the Six Human TAU Isoforms: Somatic Retention of 2N-TAU and Increased Microtubule Number Induced by 4R-TAU publication-title: Front. Neurosci. doi: 10.3389/fnins.2021.643115 contributor: fullname: Bachmann – volume: 276 start-page: 48165 year: 2001 ident: ref_13 article-title: Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure publication-title: J. Biol. Chem. doi: 10.1074/jbc.M105196200 contributor: fullname: Barghorn – volume: 112 start-page: 2758 year: 2015 ident: ref_14 article-title: Regulation and aggregation of intrinsically disordered peptides publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1418155112 contributor: fullname: Levine – volume: 133 start-page: 665 year: 2017 ident: ref_3 article-title: Roles of tau protein in health and disease publication-title: Acta Neuropathol. doi: 10.1007/s00401-017-1707-9 contributor: fullname: Guo – volume: 112 start-page: E3095 year: 2015 ident: ref_33 article-title: Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1500851112 contributor: fullname: Micsonai – volume: 5 start-page: 577 year: 2011 ident: ref_28 article-title: Trehalose: An intriguing disaccharide with potential for medical application in ophthalmology publication-title: Clin. Ophthalmol. contributor: fullname: Luyckx – volume: 18 start-page: 24 year: 2009 ident: ref_27 article-title: Effect of trehalose on protein structure publication-title: Protein Sci. doi: 10.1002/pro.3 contributor: fullname: Jain – volume: 280 start-page: 24978 year: 2005 ident: ref_8 article-title: Sites of Tau Important for Aggregation Populate β-Structure and Bind to Microtubules and Polyanions publication-title: J. Biol. Chem. doi: 10.1074/jbc.M501565200 contributor: fullname: Mukrasch – volume: 50 start-page: 9446 year: 2011 ident: ref_12 article-title: Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms publication-title: Biochemistry doi: 10.1021/bi2010569 contributor: fullname: Combs – volume: 45 start-page: 327 year: 2013 ident: ref_19 article-title: Small molecules interacting with α-synuclein: Antiaggregating and cytoprotective properties publication-title: Amino Acids doi: 10.1007/s00726-013-1503-3 contributor: fullname: Marchiani – volume: 110 start-page: E3138 year: 2013 ident: ref_17 article-title: Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1301440110 contributor: fullname: Holmes – volume: 5 start-page: 30 year: 2014 ident: ref_22 article-title: Ceftriaxone blocks the polymerization of α-synuclein and exerts neuroprotective effects in vitro publication-title: ACS Chem. Neurosci. doi: 10.1021/cn400149k contributor: fullname: Ruzza – volume: 6 start-page: 2328 year: 2021 ident: ref_36 article-title: Heparin Accelerates the Protein Aggregation via the Downhill Polymerization Mechanism: Multi-Spectroscopic Studies to Delineate the Implications on Proteinopathies publication-title: ACS Omega doi: 10.1021/acsomega.0c05638 contributor: fullname: Ahanger – ident: ref_7 doi: 10.3390/molecules25051195 – volume: 79 start-page: 474 year: 2020 ident: ref_16 article-title: Heparan Sulfate Proteoglycans Undergo Differential Expression Alterations in Alzheimer Disease Brains publication-title: J. Neuropathol. Exp. Neurol. doi: 10.1093/jnen/nlaa016 contributor: fullname: Ordiales – volume: 46 start-page: W315 year: 2018 ident: ref_32 article-title: BeStSel: A web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra publication-title: Nucleic Acids Res. doi: 10.1093/nar/gky497 contributor: fullname: Micsonai – volume: 38 start-page: 637 year: 2017 ident: ref_4 article-title: A Brief Overview of Tauopathy: Causes, Consequences, and Therapeutic Strategies publication-title: Trends Pharmacol. Sci. doi: 10.1016/j.tips.2017.03.011 contributor: fullname: Orr – volume: 26 start-page: 1085 year: 2006 ident: ref_6 article-title: Intrinsically disordered proteins in the neurodegenerative processes: Formation of tau protein paired helical filaments and their analysis publication-title: Cell Mol. Neurobiol. doi: 10.1007/s10571-006-9083-3 contributor: fullname: Skrabana – volume: 17 start-page: 83 year: 2007 ident: ref_35 article-title: Structural principles of tau and the paired helical filaments of Alzheimer’s disease publication-title: Brain Pathol. doi: 10.1111/j.1750-3639.2007.00053.x contributor: fullname: Mandelkow |
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SubjectTerms | Algae Alzheimer Disease - metabolism Alzheimer's disease Antibiotics Ceftriaxone Ceftriaxone - pharmacology Circular Dichroism Cytoskeleton Decomposition Diamonds Dichroism Filaments Food processing Heparin Humans intrinsically disordered proteins Kinetics Microtubules Neurofibrillary tangles Neurofibrillary Tangles - metabolism Peptides Peptides - chemistry Phase transitions protein aggregation Protein folding Proteins Repressor Proteins - metabolism Spectrum analysis Stability Synchrotron radiation Synchrotrons Tau protein tau Proteins - metabolism tauopathies Trehalose Trehalose - metabolism Trehalose - pharmacology |
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Title | Effect of Trehalose and Ceftriaxone on the Stability of Aggregating-Prone Tau Peptide Containing PHF6 Sequence: An SRCD Study |
URI | https://www.ncbi.nlm.nih.gov/pubmed/35328353 https://www.proquest.com/docview/2642432327 https://www.proquest.com/docview/2644013266/abstract/ https://pubmed.ncbi.nlm.nih.gov/PMC8951053 https://doaj.org/article/a8b1c83a691548b5a487b0a4e803f796 |
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