Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry

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. He...

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Main Authors:	Tae Su Choi, Hong Hee Lee, Young Ho Ko, Kwang Seob Jeong, Kimoon Kim, Hugh I. Kim
Format:	article
Language:	EN
Published:	Nature Portfolio 2017
Subjects:	Medicine R Science Q
Online Access:	https://doaj.org/article/b0e339e571fd4b16a635a34b32c9735c
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spelling	oai:doaj.org-article:b0e339e571fd4b16a635a34b32c9735c2021-12-02T15:05:49ZNanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry10.1038/s41598-017-06181-42045-2322https://doaj.org/article/b0e339e571fd4b16a635a34b32c9735c2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06181-4https://doaj.org/toc/2045-2322Abstract 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 ~40 nm to ~10 μm 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-β 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.Tae Su ChoiHong Hee LeeYoung Ho KoKwang Seob JeongKimoon KimHugh I. KimNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-7 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tae Su Choi Hong Hee Lee Young Ho Ko Kwang Seob Jeong Kimoon Kim Hugh I. Kim Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry
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 ~40 nm to ~10 μm 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-β 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.
format	article
author	Tae Su Choi Hong Hee Lee Young Ho Ko Kwang Seob Jeong Kimoon Kim Hugh I. Kim
author_facet	Tae Su Choi Hong Hee Lee Young Ho Ko Kwang Seob Jeong Kimoon Kim Hugh I. Kim
author_sort	Tae Su Choi
title	Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry
title_short	Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry
title_full	Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry
title_fullStr	Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry
title_full_unstemmed	Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry
title_sort	nanoscale control of amyloid self-assembly using protein phase transfer by host-guest chemistry
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/b0e339e571fd4b16a635a34b32c9735c
work_keys_str_mv	AT taesuchoi nanoscalecontrolofamyloidselfassemblyusingproteinphasetransferbyhostguestchemistry AT hongheelee nanoscalecontrolofamyloidselfassemblyusingproteinphasetransferbyhostguestchemistry AT younghoko nanoscalecontrolofamyloidselfassemblyusingproteinphasetransferbyhostguestchemistry AT kwangseobjeong nanoscalecontrolofamyloidselfassemblyusingproteinphasetransferbyhostguestchemistry AT kimoonkim nanoscalecontrolofamyloidselfassemblyusingproteinphasetransferbyhostguestchemistry AT hughikim nanoscalecontrolofamyloidselfassemblyusingproteinphasetransferbyhostguestchemistry
_version_	1718388725742829568

Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry

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