Amyloids are diverse group of peptides that can be found in cellular environment in both pathological and functional purposes. Their unique stable aggregates which are the critical constituents of different class of degenerative diseases provide new insights in developing new materials. In this study, we design oppositely charged amyloid inspired peptides (AIPs), which rapidly self-assemble into nanofibers at pH 7 upon mixing in water depending on noncovalent interactions. The interactions and dynamic aggregation kinetics of the peptides are analyzed via molecular dynamics simulations. Amyloid-inspired design strategy also contributes to obtain self-supporting peptide gels with remarkable mechanical properties shown in oscillatory rheology. In addition to bulk mechanical analysis of the gels, nanomechanical characterization of AIPs nanofibers is performed by double-pass force-distance mapping, which allows analysis of the adhesion and elastic properties. We also test cell-amyloid-inspired nanostructures interactions by culturing human umbilical vein endothelial cells (HUVECs) on the peptide nanofibers as a synthetic extracellular scaffold system. The encapsulation capacity of the gels is analyzed monitoring the release profile of a zwitterionic dye from AIPs networks which can be utilized to deliver biologics and small molecule drugs for medical applications. Figure 1. <img src='https://acs-archive-assets2.s3.amazonaws.com/239nm/uploads/8223_overview.jpg' alt='' />

Amyloid inspired self-assembled peptide nanofibers

246th National Meeting (2013)

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