Gel-to-Solution Transition of Sulfhydryl Self-Assembled Peptide Hydrogels Undergoing Oxidative Modulation.

Abstract

The design of self-assembling biomaterials needs to take into consideration the timing and location of the self-assembly process. In recent decades, the principal strategy has been to control the peptide self-assembly under specific conditions to enable its functional performance. However, few studies have explored the responsive elimination of functional self-assembled peptide hydrogels after their function has been performed. We designed peptide ECAFF (ECF-5), which under reductive conditions can self-assemble into a hydrogel. Upon exposure to oxidizing conditions, disulfide bonds form between the peptides, altering their molecular structure and impacting their self-assembly capability. As a result, the peptide hydrogels transition to a soluble state. This study investigates the utilization of oxidation to induce a gel-to-solution transition in peptide hydrogels and provides an explanation for their degradation following free radical treatment. Self-assembled peptide hydrogel materials can be designed from a fresh perspective by considering the degradation that takes place after functional execution.