Enzyme-responsive chiral self-sorting in amyloid-inspired minimalistic peptide amphiphiles. Issue 36 (4th September 2020)

• Record Type: Journal Article
• Authors: Gupta, Deepika; Sasmal, Ranjan; Singh, Ashmeet; Joseph, Jojo P.; Miglani, Chirag; Agasti, Sarit S.; Pal, Asish
• Is Part Of: Nanoscale. Volume 12:Issue 36(2020)
• Page Start: 18692
• Page End: 18700
• Publication Date: 2020-09-04
• Subjects: Nanoscience -- Periodicals; Nanotechnology -- Periodicals; 620.505
• DOI: 10.1039/d0nr04581k
• Languages: English
• ISSNs: 2040-3364

Abstract

Abstract : Chirality-driven self-sorting in peptide nanofibers that exhibits enantioselective enzymatic degradation for l -peptide fibers over their d -counterparts as visualized by super-resolution microscopy. Abstract : Self-sorting is a spontaneous phenomenon that ensures the formation of complex yet ordered multicomponent systems and conceptualizes the design of artificial and orthogonally functional compartments. In the present study, we envisage chirality-mediated self-sorting in β-amyloid-inspired minimalistic peptide amphiphile (C10 -l /d -VFFAKK)-based nanofibers. The fidelity and stereoselectivity of chiral self-sorting was ascertained by Förster resonance energy transfer (FRET) by the judicious choice of a pyrene (Py)-hydroxy coumarin (HOCou) donor–acceptor pair tethered to the peptide sequences. Seed-promoted elongation of the homochiral peptide amphiphiles investigated by 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 self-sorted nanofibers is reported using super-resolution microscopy that exhibits enantioselective enzymatic degradation for l -peptide fibers. Such enantioselective weakening of the hydrogels may be used for designing stimuli-responsive orthogonal compartments for delivery applications.