Towards the Design of Targeted Therapeutics based on Microbial and Antimicrobial
Amyloids, long thought to be defined by their classic cross-β fibril structure, have recently revealed a surprising new form: the cross-α architecture built from α-helices—shifting our fundamental understanding of protein self-assembly. Harnessing cutting-edge computational tools that combine secondary structure prediction with AI-driven biochemical analysis, I discovered dozens of novel amyloid-forming peptides, including unique structural variants with distinct antimicrobial functions. These findings expose the astonishing structural and functional diversity hidden within amyloids, challenging the traditional dogma that structure dictates pathology. Additionally, using sequence-based AI model we were able to correlate between various biochemical property of a sequence to the amyloid structure and function. Ultimately, this work opens new frontiers for precisely targeting pathological amyloids or designing next-generation antimicrobial agents.
