期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 138, 期 13, 页码 4362-4367出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.5b10304
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资金
- NSF [DMR-0907273]
- NIH [DP2-OD-006478-1]
- Rutgers Biotechnology Training Program (NIH) [5T32GM008339-20]
- Department of Science & Technology (DST-SERB), India [SB/FTP/PS-073/2014]
We investigate formation of nano- to micro scale peptide fibers and sheets where assembly requires association of two distinct collagen mimetic peptides (CMPs). The multicomponent nature of these designs allows the decoupling of amino acid contributions to peptide folding versus higher-order assembly. While both arginine and lysine containing CMP sequences can favor triple-helix folding, only arginine promotes rapid supramolecular assembly in each of the three two-component systems examined. Unlike lysine, the polyvalent guanidyl group of arginine is capable of both intra- and intermolecular contacts, promoting assembly. This is consistent with the supramolecular diversity of CMP morphologies observed throughout the literature. It also connects CMP self-assembly with a broad range of biomolecular interaction phenomena, providing general principles for modeling and design.
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