Computational and Experimental Investigation of the Antimicrobial Peptide Cecropin XJ and its Ligands as the Impact Factors of Antibacterial Activity

摘要: Cecropin XJ, as a heat stable antimicrobial peptide (AMP), displayed broad bacteriostatic activities, effectively inhibited proliferation of cancer cells and induced cell apoptosis in vitro. However, it exhibited little hemolytic activity very low cytotoxicity to erythrocytes normal cells. Although exerts multiple remarkable bioactivities, the refined molecular conformation native XJ remains unsolved. The aim present study is comprehensively investigate physicochemical characteristics structure-function relationship this by using series bioinformatics experimental approaches. In study, we revealed that mature consists 41 amino acids, containing two α-helical structures from Lys7 Lys25 Ala29 Ile39. phylogenetic tree indicated belongs Class I AMPs cecropin family. Hydrophobic analysis showed typical amphiphilic molecule. surface was found have much wide range electrostatic potential −83.243 +83.243. amphipathicity partially supported AMP pore-forming hypothesis. Scanning electron microscopy experimentally confirmed damages microbial membrane. Four predicted docking sites respectively for magnesium ion (Mg2+), adenosine diphosphate (ADP), bacteriopheophytin (BPH), guanosine triphosphate (GTP) were on XJ. Thereinto, Mg2+ proved suppress antibacterial XJ; both GTP ADP enhanced bactericidal activities varying degrees. provides foundation further investigation evolution, structural modification, functional mechanisms