Self-sorting is a spontaneous phenomenon that ensures formation of complex yet ordered multicomponent system and conceptualizes the design of artificial and orthogonally functional compartments. In the present study, we envisage the chirality mediated self-sorting in β-amyloid inspired minimalistic peptide amphiphiles (C10-L/D-VFFAKK) based nanofibers. The fidelity and stereo-selectivity of the chiral self-sorting was ascertained by Förster Resonance Energy Transfer (FRET) by judicious choice of pyrene-hydroxy coumarin donor-acceptor pair tethered to the peptide sequences. Seed promoted elongation of the homochiral peptide amphiphiles through AFM image analyses and Thioflavin-T (ThT) binding study further validated the chiral recognition of the L/D peptide nanofibers. Moreover, direct visualization of the chirality-driven selfsorted nanofibers are reported through super resolution microscopy that exhibits enantioselective enzymatic degradation for L-peptide fibers. Such enantioselective weakening of the hydrogels may be used in designing stimuli-responsive orthogonal compartments for delivery applications.
