Semiconductive and Biocompatible Nanofibrils from the Self-Assembly of Amyloid π-Conjugated Peptides

Abstract

Owing to their capacity to self-assemble into organized nanostructures, amyloid polypeptides can serve as scaffolds for the design of biocompatible semiconductive materials. Herein, symmetric and asymmetric amyloid π-conjugated peptides were prepared through condensation of perylene diimide (PDI) with a natural amyloidogenic sequence derived from the islet amyloid polypeptide. These PDI-bioconjugates assembled into long and linear nanofilaments in aqueous solution, which were characterized by a cross-β-sheet quaternary organization. Current−voltage curves exhibited a clear signature of semiconductors, whereas the cellular assays revealed cytocompatibility and potential application in fluorescence microscopy. Although the incorporation of a single amyloid peptide appeared sufficient to drive the selfassembly into organized fibrils, the incorporation of two peptide sequences at the PDI's imide positions significantly enhanced the conductivity of nanofibril-based films. Overall, this study exposes a novel strategy based on amyloidogenic peptide to guide the selfassembly of π-conjugated systems into robust, biocompatible, and optoelectronic nanofilaments.

Thermo-Chemical Cues-Mediated Strategy to Control Peptide Self-Assembly and Charge Transfer Complexation

“…Further, we assessed the biocompatibility of the peptide amphiphile 1 toward mice fibroblasts L929 cells, and it was found to be biocompatible (Figure S12C). − ,− Since the peptide 1 alone did not exhibit cytotoxicity, we conducted an MTT assay on the L929 mouse fibroblast cell line after forming its CT complex with TCNQ . Though TCNQ alone exhibited much reduced cell viability toward L929 fibroblast cells (Figure S12D), the CT complex exhibited no cytotoxicity to the fibroblast cells over a broad concentration regime as high as 0.64 mM (Figure B).…”

Peptide‐Based Optical/Electronic Materials: Assembly and Recent Applications in Biomedicine, Sensing, and Energy Storage

“…Current–voltage curves exhibited a clear signature of semiconductors, whereas the cellular assays revealed cytocompatibility and potential application in fluorescence microscopy. [ 71 ] Honick et al. used peptide molecules with different sequences DAIA, VEVAA, VEVFA, VEVGG, VEVFG, VEVAG, and DAVG to modulate exciton transport behavior during supramolecular assembly.…”

“…Current-voltage curves exhibited a clear signature of semiconductors, whereas the cellular assays revealed cytocompatibility and potential application in fluorescence microscopy. [71] Honick et al used peptide molecules with different sequences DAIA, VEVAA, VEVFA, VEVGG, VEVFG, VEVAG, and DAVG to modulate exciton transport behavior during supramolecular assembly. These peptides attached to PDI core were selected based on their ability to foster a wide range of excitonic coupling strengths within organized assemblies, as reflected by experimentally measured steady-state absorption and emission spectra.…”

Synthetic Multicomponent Nanovaccines Based on the Molecular Co-assembly of β-Peptides Protect against Influenza A Virus

“…We have previously reported that the self-assembly of the I 10 sequence into immunostimulatory cross-β nanofilaments tolerates the addition of long peptide epitopes 25,26 and of bulky hydrophobic compounds. 29 Herein, by adjusting the stoichiometry of the peptide monomeric building blocks, the relative density of the antigen and the TLR agonist on the nanostructure could be controlled. These multicomponent nanofilaments induced a robust epitope-specific immune response and completely protected immunized mice from a lethal viral inoculation.…”

“…In this context, we harnessed the high capacity of a 10-mer peptide sequence (I 10 ) to self-assemble into intrinsically immunostimulating nanofilaments organized in a quaternary cross-β-sheet architecture to prepare multicomponent vaccines. We have previously reported that the self-assembly of the I 10 sequence into immunostimulatory cross-β nanofilaments tolerates the addition of long peptide epitopes , and of bulky hydrophobic compounds . Herein, by adjusting the stoichiometry of the peptide monomeric building blocks, the relative density of the antigen and the TLR agonist on the nanostructure could be controlled.…”