Design, Structural Stability, Membrane Binding, and Antibacterial Activity of Novel Antimicrobial Peptides Derived from Wuchuanin-A1.

ABSTRACT: Antibiotic resistance is a major health problem globally, highlighting the need for alternative antimicrobials that may potentially reduce the emergence of resistance compared to conventional antibiotics. Antimicrobial peptides (AMPs) are promising candidates because of their broad-spectrum activity. In this study, we designed three derivatives (i.e., Analog-1, -2, and -3) of the native peptide, Wuchuanin-A1, for improving their antibacterial activity against Staphylococcus aureus and Escherichia coli. The hypothesis is that the antibacterial activity of these peptides can be improved by increasing their amphipathicity (evaluated using hydrophobic moment analysis), α-helical stability, and membrane binding properties. In this case, the residues of native peptide were mutated

SUBMITTER: Putri RA 

PROVIDER: S-EPMC12565435 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature