Phosphorylation as an Effective Tool to Improve Stability and Reduce Toxicity of Antimicrobial Peptides

J Med Chem. 2024 Nov 14;67(21):18807-18827. doi: 10.1021/acs.jmedchem.4c01179. Epub 2024 Oct 9.

Abstract

Developing a straightforward and effective strategy to modify antimicrobial peptides (AMPs) is crucial in overcoming the challenges posed by their instability and toxicity. Phosphorylation can reduce toxicity and improve the stability of AMPs. Based on these, we designed a series of peptides and their corresponding phosphorylated forms. The results showed that all phosphorylated peptides displayed reduced toxicity and enhanced stability compared to their unphosphorylated counterparts. Among them, W3BipY8-P stood out as the most promising peptide, exhibiting similar antibacterial activity as its unphosphorylated analog W3BipY8 but with significantly reduced hemolytic activity (19-fold decrease), cytotoxicity (3.3-fold decrease), and an extended serum half-life 6.3 times longer than W3BipY8. W3BipY8-P exerted bactericidal effects by disrupting bacterial membranes. Notably, W3BipY8-P significantly prolonged the survival of bacteria-infected animals while its LD50 was 4.2 times higher than that of W3BipY8. These findings highlight phosphorylation as an effective strategy for improving the antimicrobial properties of AMPs.

MeSH terms

  • Animals
  • Anti-Bacterial Agents* / chemical synthesis
  • Anti-Bacterial Agents* / chemistry
  • Anti-Bacterial Agents* / pharmacology
  • Antimicrobial Cationic Peptides / chemical synthesis
  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / pharmacology
  • Antimicrobial Peptides / chemical synthesis
  • Antimicrobial Peptides / chemistry
  • Antimicrobial Peptides / pharmacology
  • Hemolysis* / drug effects
  • Humans
  • Mice
  • Microbial Sensitivity Tests*
  • Phosphorylation / drug effects
  • Structure-Activity Relationship

Substances

  • Anti-Bacterial Agents
  • Antimicrobial Peptides
  • Antimicrobial Cationic Peptides