Issue 49, 2018

Hetero-assembly of a dual β-amyloid variant peptide system

Abstract

Self-assembly of amyloid polypeptides (1) imparts biological effects depending on the size in over 20 amyloid diseases and (2) produces useful yet relatively untapped biomaterials. Unfortunately, our understanding of amyloid polypeptides, as related to biomedical implications and biomaterial applications, is limited by their self-assembling nature. In this study, we report the creation of a dual peptide system, where a pair of β-amyloid (Aβ) variants are not self-assembled but hetero-assembled in the presence of their assembly partners. We provide evidence that the resulting hetero-assemblies share molecular, structural and morphological similarities with typical amyloid self-assemblies formed by a single polypeptide (e.g., Aβ). We anticipate that our dual peptide system may readily be adapted for precise control of amyloid assembly, for the study of size-dependent neurotoxicity and precise fabrication of amyloid biomaterials.

Graphical abstract: Hetero-assembly of a dual β-amyloid variant peptide system

Supplementary files

Article information

Article type
Communication
Submitted
04 Apr 2018
Accepted
22 May 2018
First published
25 May 2018

Chem. Commun., 2018,54, 6380-6383

Author version available

Hetero-assembly of a dual β-amyloid variant peptide system

J. Candreva, E. Chau, E. Aoraha, V. Nanda and J. R. Kim, Chem. Commun., 2018, 54, 6380 DOI: 10.1039/C8CC02724B

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