Design and function analysis of novel antimicrobial peptides derived from Cathelicidin-DM: Insights into structure-function relationships.

The increasing threat of bacterial drug resistance calls for effective solutions, and antimicrobial peptides (AMPs) hold great promise. However, the connection between their structure and function remains unclear. The study of the structure-function relationship and other basic issues of AMPs is a guarantee for the development of safe, effective and clear mechanism of therapeutic drugs or active biomaterials. The aim of this study was to develop new antimicrobial candidate molecules and further elucidate the structure-function relationship of AMPs. In this study, more than 20 AMPs derived from Cathelicidin-DM were designed in terms of sequence size, amino acid composition, amphiphilicity and amidation. And then the antimicrobial activity in vitro/vivo, structure of peptides, safety and stability assessment, antimicrobial mechanism, anti-inflammatory activity, and in vivo toxicity were evaluated, and the relationship between structure and function of AMPs was analyzed. The results showed that the hydrophobicity amino acid substitution is of great significance to improve the biological activity of AMPs. Overall, our research uncovers the potential link between the function and structure of AMPs, laid the foundation for the development of AMPs drugs and biomaterials.