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dc.contributor.authorCheung, David L.
dc.date.accessioned2020-09-09T13:35:08Z
dc.date.available2020-09-09T13:35:08Z
dc.date.issued2020-09-04
dc.identifier.citationCheung, David L. (2020). Effect of surface chemistry on islet amyloid polypeptide conformation. Biointerphases, 15(5), 051001. doi:10.1116/6.0000417en_IE
dc.identifier.issn1559-4106
dc.identifier.urihttp://hdl.handle.net/10379/16168
dc.description.abstractThe formation of dense, linear arrays (fibrils) by biomolecules is the hallmark of a number of degenerative diseases, such as Alzheimer s and type-2 diabetes. Protein fibrils have also attracted interest as building blocks for new materials. It has long been recognized that surfaces can affect the fibrillation process. Recent work on the model fibril forming protein human islet amyloid polypeptide (hIAPP) has shown that while the protein concentration is highest at hydrophobic surfaces, the rate of fibril formation is lower than on other surfaces. To understand this, replica exchange molecular dynamics simulations were used to investigate the conformations that hIAPP adopts on surfaces of different hydrophobicities. The hydrophobic surface stabilizes α-helical structures which are significantly different to those found on the hydrophilic surface and in bulk solution. There is also a greatly reduced conformational ensemble on the hydrophobic surface due to long-lived contacts between hydrophobic residues on the protein and the surface. This new microscopic information will help us determine the mechanism of the enhancement of fibril formation on surfaces and provides new insight into the effect of nanointerfaces and protein conformation.en_IE
dc.description.sponsorshipComputational facilities for this work were provided by the SFI/HEA funded Irish Centre for High End Computing. Atomic structures for hIAPP in fibrils were provided by Robert Tycko (NIH). The author wishes to thank Kieran Somers for useful discussions during this work.en_IE
dc.formatapplication/pdfen_IE
dc.language.isoenen_IE
dc.publisherAmerican Institute of Physicsen_IE
dc.relation.ispartofBiointerphasesen
dc.subjectsurface chemistryen_IE
dc.subjectislet amyloid polypeptide conformationen_IE
dc.subjectChemistryen_IE
dc.subjectProtein structureen_IE
dc.subjectMolecular dynamicsen_IE
dc.subjectComputational modelsen_IE
dc.subjectAmyloidsen_IE
dc.subjectData visualizationen_IE
dc.subjectHydrophobic effecten_IE
dc.subjectPolypeptideen_IE
dc.subjectSurface and interface chemistryen_IE
dc.subjectDiseases and conditionsen_IE
dc.subjectBiomaterialsen_IE
dc.titleEffect of surface chemistry on islet amyloid polypeptide conformationen_IE
dc.typeArticleen_IE
dc.date.updated2020-09-08T15:24:53Z
dc.identifier.doi10.1116/6.0000417
dc.local.publishedsourcehttps://doi.org/10.1116/6.0000417en_IE
dc.description.peer-reviewedpeer-reviewed
dc.internal.rssid22586563
dc.local.contactDavid Cheung, School Of Chemistry, Nuig. Email: david.cheung@nuigalway.ie
dc.local.copyrightcheckedYes
dc.local.versionACCEPTED
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