Interactions of Peptide Amphiphiles With Viruses and Cells Are Enabled by Amorphous Nanostructures.

Abstract

Peptide amphiphiles can form fibrillar and amorphous structures. While fibrillar assemblies have previously been shown to enhance viral infectivity or retroviral transduction for gene delivery, we now elucidate the mechanism behind amorphous peptide amphiphiles that promote virus-cell interactions. Using electron microscopy, we reveal that amorphous fragments of polyunsaturated peptide amphiphiles allow for more VLPs to bind directly to the plasma membrane, explaining previously observed efficient viral entry and superior biodegradation compared to state-of-the-art adjuvants. We believe our work highlights the potential of unsaturated fatty acid peptide hybrid materials for clinical applications.