Nanoscale Control of Amyloid Self Assembly Using Protein Phase Transfer by Host-Guest Chemistry
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Choi, Tae Su | - |
dc.contributor.author | Lee, Hong Hee | - |
dc.contributor.author | Ko, Young Ho | - |
dc.contributor.author | Jeong, Kwang Seob | - |
dc.contributor.author | Kim, Kimoon | - |
dc.contributor.author | Kim, Hugh I. | - |
dc.date.accessioned | 2021-09-03T03:51:06Z | - |
dc.date.available | 2021-09-03T03:51:06Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2017-07-18 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/82815 | - |
dc.description.abstract | Amyloid fibrils have recently been highlighted for their diverse applications as functional nanomaterials in modern chemistry. However, tight control to obtain a targeted fibril length with low heterogeneity has not been achieved because of the complicated nature of amyloid fibrillation. Herein, we demonstrate that fibril assemblies can be homogeneously manipulated with desired lengths from similar to 40 nm to similar to 10 mu m by a phase transfer of amyloid proteins based on host-guest chemistry. We suggest that host-guest interactions with cucurbit[6] uril induce a phase transfer of amyloid proteins (human insulin, human islet amyloid polypeptide, hen egg lysozyme, and amyloid-beta 1-40 & 1-42) from the soluble state to insoluble state when the amount of cucurbit[6] uril exceeds its solubility limit in solution. The phase transfer of the proteins kinetically delays the nucleation of amyloid proteins, while the nuclei formed in the early stage are homogeneously assembled to fibrils. Consequently, supramolecular assemblies of amyloid proteins with heterogeneous kinetics can be controlled by protein phase transfer based on host-guest interactions. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.subject | MOLECULAR RECOGNITION | - |
dc.subject | BOVINE INSULIN | - |
dc.subject | FIBRILLATION | - |
dc.subject | MECHANISM | - |
dc.subject | SUPERSATURATION | - |
dc.subject | INTERMEDIATE | - |
dc.subject | CUCURBITURIL | - |
dc.subject | MEMBRANES | - |
dc.subject | KINETICS | - |
dc.title | Nanoscale Control of Amyloid Self Assembly Using Protein Phase Transfer by Host-Guest Chemistry | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Jeong, Kwang Seob | - |
dc.contributor.affiliatedAuthor | Kim, Hugh I. | - |
dc.identifier.doi | 10.1038/s41598-017-06181-4 | - |
dc.identifier.scopusid | 2-s2.0-85024921416 | - |
dc.identifier.wosid | 000405746500021 | - |
dc.identifier.bibliographicCitation | SCIENTIFIC REPORTS, v.7 | - |
dc.relation.isPartOf | SCIENTIFIC REPORTS | - |
dc.citation.title | SCIENTIFIC REPORTS | - |
dc.citation.volume | 7 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | MOLECULAR RECOGNITION | - |
dc.subject.keywordPlus | BOVINE INSULIN | - |
dc.subject.keywordPlus | FIBRILLATION | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | SUPERSATURATION | - |
dc.subject.keywordPlus | INTERMEDIATE | - |
dc.subject.keywordPlus | CUCURBITURIL | - |
dc.subject.keywordPlus | MEMBRANES | - |
dc.subject.keywordPlus | KINETICS | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(02841) 서울특별시 성북구 안암로 14502-3290-1114
COPYRIGHT © 2021 Korea University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.