Study On Interaction Between Self-assembled Nano Antibacterial Peptide C₁₆-OH-CATH20 And Vesicle Interface

Drug-resistant bacterial infections have become one of the top ten global public threats to human health.Therefore,the research and development of new antibacterial drugs is an urgent problem to be solved.Antimicrobial peptides have attracted wide attention and become a research hotspot due to their advantages of low toxicity,high antibacterial activity,controllable structure and low resistance to drugs.In this paper,self-assembled nano-sized antibacterial peptide C₁₆-OH-CATH20（NAs）was prepared by combining palmitic acid with Cathlicidins family antibacterial peptide OH-CATH20（Pep20）by polypeptide solid phase synthesis method,and its antibacterial activity and antibacterial mechanism were studied.The main results are as follows:（1）Using wang resin as carrier,antimicrobial peptide NAs was successfully prepared by polypeptide solid phase synthesis.（2）In vitro activity test against drug-resistant bacteria showed that NAs had high activity and antibacterial efficiency against E.coli MDR.（3）The morphology,membrane curvature and membrane potential of vesicles were measured and it was found that NAs could strongly disturb bacterial membranes,thus damaging the integrity of membrane structure and increasing membrane permeability.（4）The test of E.coli MDR showed that the membrane surface appeared folds and depressions under the action of NAs,the permeability of bacterial membrane increased,and even the phenomenon of bacterial content outflow.This study theoretically helps to clarify the antimicrobial activity of self-assembled nano antimicrobial peptide NAs against drug-resistant bacteria and the specific mechanism of action against E.coli MDR,and provides a theoretical basis for the further study of antimicrobial peptides against drug-resistant bacteria.