Design of Multicomponent Peptide Fibrils with Ordered and Programmable Compositional Patterns

Author:

Cheng Dan1,Chen Xin1,Zhang Weijia1,Guo Pan1,Xue Wenhui2,Xia Junfan3,Wu Siyu4,Shi Junhui5,Ma Dan5,Zuo Xiaobing4,Jiang Bin3,Li Shaowei2,Xia Ningshao2,Jiang Yunbao16,Conticello Vincent P.7,Jiang Tao16ORCID

Affiliation:

1. Department of Chemistry Collage of Chemistry and Chemical Engineering Xiamen University The MOE Key Laboratory of Spectrochemical Analysis and Instrumentation Xiamen 361005 China

2. State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics National Institute of Diagnostics and Vaccine Development in Infectious Disease School of Life Sciences School of Public Health Xiamen University Xiamen 361102 China

3. Department of Chemical Physicals University of Science and Technology of China Hefei 230026 China

4. X-ray Science Division Argonne National Laboratory Lemont IL 60439 USA

5. Key Laboratory of Structural Biology of Zhejiang Province School of Life Sciences Westlake University Hangzhou 310024 China

6. Innovation Laboratory for Sciences and Technologies of Energy Materials of Fujian Province (IKKEM) Xiamen 361005 China

7. Department of Chemistry Emory University Atlanta GA 30033 USA

Abstract

AbstractAdvanced applications of biomacromolecular assemblies require a stringent degree of control over molecular arrangement, which is a challenge to current synthetic methods. Here we used a neighbor‐controlled patterning strategy to build multicomponent peptide fibrils with an unprecedented capacity to manipulate local composition and peptide positions. Eight peptides were designed to have regulable nearest neighbors upon co‐assembly, which, by simulation, afforded 412 different patterns within fibrils, with varied compositions and/or peptide positions. The fibrils with six prescribed patterns were experimentally constructed with high accuracy. The controlled patterning also applies to functionalities appended to the peptides, as exemplified by arranging carbohydrate ligands at nanoscale precision for protein recognition. This study offers a route to molecular editing of inner structures of peptide assemblies, prefiguring the uniqueness and richness of patterning‐based material design.

Funder

National Natural Science Foundation of China

Fundamental Research Funds for the Central Universities

Publisher

Wiley

Subject

General Chemistry,Catalysis

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