Journal
CHEM
Volume 4, Issue 8, Pages 1862-1876Publisher
CELL PRESS
DOI: 10.1016/j.chempr.2018.05.016
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Funding
- Italian Ministry of University and Research through Scientific Independence of young Researchers program (HOT-SPOT) [RBSI14A7PL]
- Ramon Areces Foundation
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Self-assembling short peptides are attractive minimal systems for mimicking the constituents of living systems and building (bio) materials. The combination of both D-and L-amino acids into heterochiral sequences is a versatile strategy for building durable supramolecular architectures, especially when their homochiral analogs do not self-assemble. The reasons for this divergent behavior have remained obscure until now. Here, we elucidate how and why homochiral and heterochiral peptides behave differently. We identify a key spectroscopy signature and its corresponding molecular conformation, whereby an amphiphilic structure is uniquely enabled by the peptide stereochemistry. Importantly, we unravel the self-assembly process as a continuum from the conformation of single molecules to their organization into nano-andmicrostructures and through to macroscopic hydrogels, which are probed for cytotoxicity in fibroblast cell culture. In this way, (bio) material properties at the macro-scale can be linked to the chemical structure of their building blocks at the angstrom scale.
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