DC Field | Value | Language |
---|---|---|
dc.contributor.author | Tae Su Choi | - |
dc.contributor.author | Jong Wha Lee | - |
dc.contributor.author | Kyeong Sik Jin | - |
dc.contributor.author | Kim, HI | - |
dc.date.accessioned | 2015-06-25T01:34:19Z | - |
dc.date.available | 2015-06-25T01:34:19Z | - |
dc.date.created | 2015-02-10 | - |
dc.date.issued | 2014-10-21 | - |
dc.identifier.issn | 0006-3495 | - |
dc.identifier.other | 2015-OAK-0000031885 | en_US |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/9847 | - |
dc.description.abstract | Amyloid fibrillation in water-organic mixtures has been widely studied to understand the effect of protein-solvent interactions on the fibrillation process. In this study, we monitored insulin fibrillation in formamide and its methyl derivatives (formamide, N-methyl formamide, N,N-dimethyl formamide) in the presence and absence of water. These model solvent systems mimic the cellular environment by providing denaturing conditions and a hydrophobic environment with limited water content. Thioflavin T (ThT) assay revealed that binary mixtures of water with formamide and its methyl derivatives enhanced fibrillation rates and beta-sheet abundance, whereas organic solvents suppressed insulin fibrillation. We utilized solution small-angle x-ray scattering (SAXS) and differential scanning calorimetry (DSC) to investigate the correlation between protein-solvent interactions and insulin fibrillation. SAXS experiments combined with simulated annealing of the protein indicated that the degree of denaturation of the hydrophobic core region at residues B11-B17 determines the fibrillation rate. In addition, DSC experiments suggested a crucial role of hydrophobic interactions in the fibrillation process. These results imply that an environment with limited water, which imitates a lipid membrane system, accelerates protein denaturation and the formation of intermolecular hydrophobic interactions during amyloid fibrillation. | - |
dc.description.statementofresponsibility | open | en_US |
dc.language | English | - |
dc.publisher | Cell Press | - |
dc.relation.isPartOf | BIOPHYSICAL JOURNAL | - |
dc.rights | BY_NC_ND | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/2.0/kr | en_US |
dc.title | Amyloid Fibrillation of Insulin under Water-Limited Conditions | - |
dc.type | Article | - |
dc.contributor.college | 첨단재료과학부 | en_US |
dc.identifier.doi | 10.1016/J.BPJ.2014.09.008 | - |
dc.author.google | Choi, TS | en_US |
dc.author.google | Lee, JW | en_US |
dc.author.google | Kim, HI | en_US |
dc.author.google | Jin, KS | en_US |
dc.relation.volume | 107 | en_US |
dc.relation.issue | 8 | en_US |
dc.relation.startpage | 1939 | en_US |
dc.relation.lastpage | 1949 | en_US |
dc.contributor.id | 10652893 | en_US |
dc.relation.journal | BIOPHYSICAL JOURNAL | en_US |
dc.relation.index | SCI급, SCOPUS 등재논문 | en_US |
dc.relation.sci | SCI | en_US |
dc.collections.name | Journal Papers | en_US |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | BIOPHYSICAL JOURNAL, v.107, no.8, pp.1939 - 1949 | - |
dc.identifier.wosid | 000343682700020 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 1949 | - |
dc.citation.number | 8 | - |
dc.citation.startPage | 1939 | - |
dc.citation.title | BIOPHYSICAL JOURNAL | - |
dc.citation.volume | 107 | - |
dc.contributor.affiliatedAuthor | Kim, HI | - |
dc.identifier.scopusid | 2-s2.0-84908225375 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 10 | - |
dc.description.scptc | 11 | * |
dc.date.scptcdate | 2018-10-274 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | X-RAY SOLUTION | - |
dc.subject.keywordPlus | ALPHA-SYNUCLEIN | - |
dc.subject.keywordPlus | INTERFACIAL REACTIONS | - |
dc.subject.keywordPlus | PROTEIN AGGREGATION | - |
dc.subject.keywordPlus | THIOFLAVIN-T | - |
dc.subject.keywordPlus | STRUCTURAL-CHARACTERIZATION | - |
dc.subject.keywordPlus | GLOBULAR-PROTEINS | - |
dc.subject.keywordPlus | ORGANIC-SOLVENTS | - |
dc.subject.keywordPlus | MOLECULAR-BASIS | - |
dc.subject.keywordPlus | LIPID-BILAYERS | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biophysics | - |
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