Characterizing Amyloid-Beta Protein Misfolding From Molecular Dynamics Simulations With Explicit Water
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Chewook | - |
dc.contributor.author | Ham, Sihyun | - |
dc.date.available | 2021-02-22T13:18:39Z | - |
dc.date.issued | 2011-01 | - |
dc.identifier.issn | 0192-8651 | - |
dc.identifier.issn | 1096-987X | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/12697 | - |
dc.description.abstract | Extracellular deposition of amyloid-beta (A beta) protein, a fragment of membrane glycoprotein called beta-amyloid precursor transmembrane protein (beta APP), is the major characteristic for the Alzheimer's disease (AD). However, the structural and mechanistic information of forming Ab protein aggregates in a lag phase in cell exterior has been still limited. Here, we have performed multiple all-atom molecular dynamics simulations for physiological 42-residue amyloid-beta protein (A beta 42) in explicit water to characterize most plausible aggregation-prone structure (APS) for the monomer and the very early conformational transitions for A beta 42 protein misfolding process in a lag phase. Monitoring the early sequential conformational transitions of A beta 42 misfolding in water, the APS for A beta 42 monomer is characterized by the observed correlation between the nonlocal backbone H-bond formation and the hydrophobic side-chain exposure. Characteristics on the nature of the APS of A beta 42 allow us to provide new insight into the higher aggregation propensity of A beta 42 over A beta 40, which is in agreement with the experiments. On the basis of the structural features of APS, we propose a plausible aggregation mechanism from APS of A beta 42 to form fibril. The structural and mechanistic observations based on these simulations agree with the recent NMR experiments and provide the driving force and structural origin for the A beta 42 aggregation process to cause AD. (C) 2010 Wiley Periodicals, Inc. J Comput Chem 32: 349-355, 2011 | - |
dc.format.extent | 7 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | WILEY-BLACKWELL | - |
dc.title | Characterizing Amyloid-Beta Protein Misfolding From Molecular Dynamics Simulations With Explicit Water | - |
dc.type | Article | - |
dc.publisher.location | 미국 | - |
dc.identifier.doi | 10.1002/jcc.21628 | - |
dc.identifier.scopusid | 2-s2.0-78650086243 | - |
dc.identifier.wosid | 000285312300016 | - |
dc.identifier.bibliographicCitation | JOURNAL OF COMPUTATIONAL CHEMISTRY, v.32, no.2, pp 349 - 355 | - |
dc.citation.title | JOURNAL OF COMPUTATIONAL CHEMISTRY | - |
dc.citation.volume | 32 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 349 | - |
dc.citation.endPage | 355 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | sci | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.subject.keywordPlus | ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | IN-SILICO | - |
dc.subject.keywordPlus | HUNTINGTONS-DISEASE | - |
dc.subject.keywordPlus | SECONDARY STRUCTURE | - |
dc.subject.keywordPlus | AQUEOUS-SOLUTION | - |
dc.subject.keywordPlus | DIMER FORMATION | - |
dc.subject.keywordPlus | C-TERMINUS | - |
dc.subject.keywordPlus | WILD-TYPE | - |
dc.subject.keywordPlus | PEPTIDE | - |
dc.subject.keywordPlus | OLIGOMERS | - |
dc.subject.keywordAuthor | Alzheimer's disease | - |
dc.subject.keywordAuthor | protein aggregation | - |
dc.subject.keywordAuthor | protein misfolding | - |
dc.subject.keywordAuthor | aggregation-prone structure | - |
dc.subject.keywordAuthor | amyloid-beta protein | - |
dc.identifier.url | https://onlinelibrary.wiley.com/doi/full/10.1002/jcc.21628 | - |
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