Assembly of short amphiphilic peptoids into nanohelices with controllable supramolecular chirality.

Autor: Zheng R; Department of Chemical Engineering, University of Washington, Seattle, WA, 98195, USA.; Physical Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA., Zhao M; Pritzker School of Molecular Engineering, University of Chicago, Chicago, IL, 60637, USA., Du JS; Physical Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA., Sudarshan TR; School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA, 30332, USA., Zhou Y; Physical Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA., Paravastu AK; School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA, 30332, USA.; Parker H. Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology, Atlanta, GA, 30332, USA., De Yoreo JJ; Physical Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA.; Department of Materials Science, University of Washington, Seattle, WA, 98195, USA., Ferguson AL; Pritzker School of Molecular Engineering, University of Chicago, Chicago, IL, 60637, USA., Chen CL; Department of Chemical Engineering, University of Washington, Seattle, WA, 98195, USA. Chunlong.Chen@pnnl.gov.; Physical Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA. Chunlong.Chen@pnnl.gov.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2024 Apr 16; Vol. 15 (1), pp. 3264. Date of Electronic Publication: 2024 Apr 16.
DOI: 10.1038/s41467-024-46839-y
Abstrakt: A long-standing challenge in bioinspired materials is to design and synthesize synthetic materials that mimic the sophisticated structures and functions of natural biomaterials, such as helical protein assemblies that are important in biological systems. Herein, we report the formation of a series of nanohelices from a type of well-developed protein-mimetics called peptoids. We demonstrate that nanohelix structures and supramolecular chirality can be well-controlled through the side-chain chemistry. Specifically, the ionic effects on peptoids from varying the polar side-chain groups result in the formation of either single helical fiber or hierarchically stacked helical bundles. We also demonstrate that the supramolecular chirality of assembled peptoid helices can be controlled by modifying assembling peptoids with a single chiral amino acid side chain. Computational simulations and theoretical modeling predict that minimizing exposure of hydrophobic domains within a twisted helical form presents the most thermodynamically favorable packing of these amphiphilic peptoids and suggests a key role for both polar and hydrophobic domains on nanohelix formation. Our findings establish a platform to design and synthesize chiral functional materials using sequence-defined synthetic polymers.
(© 2024. Battelle Memorial Institute.)
Databáze: MEDLINE
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