Modifying the surface of peptide nanofibers utilizing a thiol‐thioester exchange

Abstract

Herein, we report on the incorporation of a dithioester modification to a self‐assembling peptide and characterize a thiol‐thioester exchange on the nanofiber's surface with respect to amount of soluble exogenous thiol present and pH of the reaction. The ratios of all peptide species throughout the exchange reaction were reproducibly monitored by matrix‐assisted laser desorption ionization time‐of‐flight (MALDI‐TOF) mass spectrometry, highlighting the utility of MALDI to characterize heterogeneous and dynamic supramolecular systems. The tuneable revealing of thiols through a dynamic covalent chemical reaction presents a new strategy for labeling supramolecular surfaces. This strategy of combining reversible peptide self‐assembly and dynamic covalent chemistry opens another route for the post‐assembly modification of amyloid‐based supramolecular structures and the design of functional biomaterials.

Access to Advanced Functional Materials through Postmodification of Biomimetic Assemblies via Click Chemistry

“…Self-assembled peptide-based nanostructures are typically modified using native chemical ligation (NCL), a chemoselective reaction that occurs between peptides or protein fragments to form a native peptide bond under mild conditions. ,, Split protein strategy, biomolecular recognition, thiol–thiolester exchange, and hydrazone formation have also been used to enable postassembly functionalization of peptide-based self-assemblies. With regard to click chemistry, CuAAC has been widely employed for cyclization and orthogonal modification of peptides on resin − but appears less prevalent for postmodification of peptide assemblies.…”