Dynamic Control of Cyclic Peptide Assembly to Form Higher‐Order Assemblies

Author:

Wu Chongyang1ORCID,Zhang Hongyue1,Kong Nan1,Wu Bihan1,Lin Xinhui1,Wang Huaimin12ORCID

Affiliation:

1. Key Laboratory of Precise Synthesis of Functional Molecules of Zhejiang Province Department of Chemistry School of Science Westlake University Institute of Natural Sciences Westlake Institute for Advanced Study No. 600 Dunyu Road Hangzhou 310024 Zhejiang Province China

2. Westlake Laboratory of Life Sciences and Biomedicine School of Life Sciences Westlake University Hangzhou 310024 Zhejiang China

Abstract

AbstractChirality correction, asymmetry, ring‐chain tautomerism and hierarchical assemblies are fundamental phenomena in nature. They are geometrically related and may impact the biological roles of a protein or other supermolecules. It is challenging to study those behaviors within an artificial system due to the complexity of displaying these features. Herein, we design an alternating D,L peptide to recreate and validate the naturally occurring chirality inversion prior to cyclization in water. The resulting asymmetrical cyclic peptide containing a 4‐imidazolidinone ring provides an excellent platform to study the ring‐chain tautomerism, thermostability and dynamic assembly of the nanostructures. Different from traditional cyclic D,L peptides, the formation of 4‐imidazolidinone promotes the formation of intertwined nanostructures. Analysis of the nanostructures confirmed the left‐handedness, representing chirality induced self‐assembly. This proves that a rationally designed peptide can mimic multiple natural phenomena and could promote the development of functional biomaterials, catalysts, antibiotics, and supermolecules.

Funder

National Natural Science Foundation of China

Publisher

Wiley

Subject

General Medicine

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