Strategy to control the process of self-assembly

Self- assembly is a key principle for the existence of viral capsids, pathogenic amyloids, gels and functional amyloids. These molecules look different at the molecular level yet the main driving forces for their existence are the interactions of amino acids within a single protein molecule and between different protein molecules. It is a well-documented fact that amyloids are responsible for various pathogenic conditions viz. cancer and neurodegeneration. Alongside, these pathogenic amyloids exist, model systems like silk that provide ample opportunities to understand and unravel the mechanism of formation and control of self –assembly of amyloids. Combining the findings of ability of diphenylalanine and benzoylated diphenylalanine to form nanotubes and spheres respectively with silk, we designed silk derived peptides with increased content of aromatic amino acids. Our findings from aggregation kinetics, AFM, TEM and FT-IR reveals the striking differences in their morphology, their possible mechanisms and hydrogen bonding abilities.