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...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2017-07-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-017-06181-4 |
| _version_ | 1819036061432545280 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-21T07:59:32Z |
| format | Article |
| id | doaj.art-b0e339e571fd4b16a635a34b32c9735c |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-21T07:59:32Z |
| publishDate | 2017-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-b0e339e571fd4b16a635a34b32c9735c2022-12-21T19:10:56ZengNature PortfolioScientific Reports2045-23222017-07-01711710.1038/s41598-017-06181-4Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest ChemistryTae Su Choi0Hong Hee Lee1Young Ho Ko2Kwang Seob Jeong3Kimoon Kim4Hugh I. Kim5Department of Chemistry, Korea UniversityDivision of Metrology for Quality of Life, Korea Research Institute of Standards and ScienceCenter for Self-assembly and Complexity, Institute for Basic ScienceDepartment of Chemistry, Korea UniversityDepartment of Chemistry, Pohang University of Science and Technology (POSTECH)Department of Chemistry, Korea UniversityAbstract 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.https://doi.org/10.1038/s41598-017-06181-4 |
| spellingShingle | 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 Scientific Reports |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s41598-017-06181-4 |
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