Chirality Effects on Peptide Self-Assembly Unraveled from Molecules to Materials

By A. M. Garcia, Daniel Iglesias, Evelina Parisi, K. Styan, Lynne J. Waddington, Caterina Deganutti, Rita De Zorzi, M. Grassi, M. Melchionna, A. Vargiu and 1 more. Chem, 2018

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Summary 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- and microstructures 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.

Subfields: Biomaterials, Molecular Biology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/f682453fe76032649fab3085556d4e16750c777c