Cross β Amyloid Nanotubes as Chiral Protoenzyme

Priyanshu, . (2022) Cross β Amyloid Nanotubes as Chiral Protoenzyme. Masters thesis, Indian Institute of Science Education and Research Kolkata.

Text (MS dissertation of Priyanshu (17MS205)) 17MS205_Thesis_file.pdf - Submitted Version Restricted to Repository staff only Download (2MB)

Abstract

Homochirality in biology, i.e., exclusive left-handed amino acids and right-handed sugars, is critical for molecular recognition and replication. This symmetry breaking in the evolution of life is believed to have originated from random excess of enantiomers, which somehow amplified to provide a homochiral biosphere. Short peptide-based amyloids capable of accessing inherent repetitive structures have been argued as the primitive protein folds. Herein, we show amyloid-based microphases featuring solvent-exposed dual residues, lysines, and imidazoles that could show selective covalent interactions with one enantiomer over another via Schiff base formation and execute enantioselective hydrolysis thus resulting in symmetry breaking. This work highlights the unique capabilities of amyloid assemblies to demonstrate enantioselective catalysis and reinforces their importance in the origin of homochirality in the prebiotic earth.

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