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Amphipathic β-sheet peptides that assemble into cross-β bilayer fibrils have been widely applied as functional biomaterials [1]. We recently discovered that enantiomeric Dand L-Ac-(FKFE)2-NH2 peptides readily coassemble into two-component “rippled β-sheet” fibrils (see Figure 1) [2] (as opposed to classical pleated β-sheet materials), consistent with Pauling’s prediction for mixtures of enantiomeric β-sheet peptides [3]. Coassembly was confirmed by isotope-edited IR spectroscopy and FRET-based fluorescence spectroscopy. The preference for coassembly into rippled β-sheets relative to self-sorting into pleated β-sheets is thermodynamically favored. Rippled β-sheet fibrils have unique emergent properties compared to pleated β-sheet fibrils, including enhanced hydrogel elasticity and resistance to protease degradation [4].

Rippled β-Sheet Fibrils from Coassembled Enantiomeric Amphipathic Peptides as Potential Microbicide Biomaterials