[Research progress in anti-enzymatic antimicrobial peptides].

Area of Science:

• Biochemistry
• Immunology
• Drug Discovery

Background:

• Antimicrobial peptides (AMPs) are vital components of the innate immune system, offering broad-spectrum activity and low resistance development.
• Natural AMPs face significant challenges in vivo due to rapid degradation by digestive enzymes, limiting their therapeutic potential.
• Enhancing AMP stability is critical for developing effective antimicrobial therapies.

Purpose of the Study:

• To review and summarize current strategies for improving the stability of antimicrobial peptides (AMPs) against protease degradation.
• To provide a comprehensive overview of techniques that enhance AMP resistance to enzymatic breakdown.
• To serve as a reference for researchers aiming to develop more stable and effective AMP-based drugs.

Main Methods:

• Incorporation of unnatural amino acids into AMP structures.
• Chemical modifications to protect AMPs from enzymatic cleavage.
• Strategic design to avoid protease recognition and cleavage sites.
• Cyclization of peptide chains to increase structural integrity.
• Development of nano-peptide formulations for enhanced stability.

Main Results:

• Various methods effectively increase the resistance of AMPs to protease degradation.
• Unnatural amino acids, chemical modifications, and cyclization are promising approaches.
• Nano-peptide design offers a novel strategy for improving AMP stability and delivery.
• These enhancements are crucial for overcoming the limitations of natural AMPs in therapeutic applications.

Conclusions:

• Improving AMP stability is achievable through diverse chemical and structural modifications.
• These strategies hold significant promise for the development of next-generation antimicrobial drugs.
• Further research into these methods will accelerate the clinical translation of AMP-based therapies.