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

ACS Appl Bio Mater. 2023 Dec 18;6(12):5836-5841. doi: 10.1021/acsabm.3c00932. Epub 2023 Nov 28.

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.

Keywords: Raman spectra; disulfide; hydrogel; oxidation−reduction; self-assembly peptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocompatible Materials / chemistry
  • Hydrogels* / chemistry
  • Oxidation-Reduction
  • Oxidative Stress
  • Peptides* / chemistry
  • Sulfhydryl Compounds

Substances

  • Hydrogels
  • Peptides
  • Biocompatible Materials
  • Sulfhydryl Compounds