Characterizations of amyloid like structures with converging approaches are important to understand their complex self-assembly mechanism and the causes of strong mechanical stability. In addition, predictable molecular organization, kinetics and mechanism of self-assembly processes are quite important in the context of designing novel supramolecular peptide nanostructures. Here, we analyzed <i>in situ</i> co-assembly kinetics of oppositely charged Amyloid Inspired Peptides (AIPs) to monitor time dependent nanofiber formation and sol-gel transition at different peptide concentration by SAXS and different techniques. The kinetics of AIPs nanostructure formation and detailed SAXS analysis of AIPs hydrogels was used to develop a structural model for co-assembled AIPs nanostructures. Increased knowledge on molecular kinetics of co-assembly of AIPs can facilitate the further modification of the designed structures, the development of therapeutic strategies for protein-folding disorders and advances in improved materials inspired from self-assembly of functional and pathological amyloids.

Time and concentration dependent assembly of amyloid-like peptides into supramolecular nanostructures

250th National Meeting (2015)

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