Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 58, Issue 23, Pages 7778-7782Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201903259
Keywords
foldamers; halogen bonding; peptides; self-assembly; structure elucidation
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Funding
- NSF CAREER [1351265]
- NIH [1R01GM112652-01A1]
- NSF MRI [CHE-1531590]
- National Science Foundation [NSF/CHE-1346572, NSF/DMR-1531283]
- Division of Chemistry (CHE) [NSF/CHE-1346572, NSF/DMR-1531283]
- Division of Materials Research (DMR) [NSF/CHE-1346572, NSF/DMR-1531283]
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Peptide-mediated self-assembly is a prevalent method for creating highly ordered supramolecular architectures. Herein, we report the first example of orthogonal C-X...X-C/C-X...pi halogen bonding and hydrogen bonding driven crystalline architectures based on synthetic helical peptides bearing hybrids of l-sulfono-gamma-AApeptides and natural amino acids. The combination of halogen bonding, intra-/intermolecular hydrogen bonding, and intermolecular hydrophobic interactions enabled novel 3D supramolecular assembly. The orthogonal halogen bonding in the supramolecular architecture exerts a novel mechanism for the self-assembly of synthetic peptide foldamers and gives new insights into molecular recognition, supramolecular design, and rational design of biomimetic structures.
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