Development of disulfide bond crosslinked antimicrobial peptide hydrogel

In the past decades, antimicrobial peptides have emerged as potential candidates as antimicrobial agents, and antimicrobial peptide-based hydrogels have been extensively studied as wound dressings or fillers. In this work, a PAF26 peptide derivative with a cysteine amino acid on the C-terminal was designed to develop covalently crosslinked antimicrobial hydrogel. The hydrogel could be formed in neutral solution and thiol in the cysteine residue could be oxidised to disulfide bond in the hydrogel. It was confirmed that the formed hydrogel had strongly crosslinked networks with beta-sheet and unordered coil secondary structures. In addition, antimicrobial experiments demonstrated that the formed hydrogel had excellent antimicrobial abilities via Candida albicans and could inhibit the growth of Staphylococcus aureus and Escherichia coli, gives the possibility of being used for fungi and bacteria-induced infection.

Automated summary

In this study, a cysteine-containing PAF26 peptide derivative was designed to develop a covalently crosslinked antimicrobial hydrogel, which showed strong crosslinked networks and excellent antimicrobial abilities against Candida albicans, Staphylococcus aureus, and Escherichia coli.