Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysaccharide binding protein from rabbit leukocytes

FEBS Letters

Gennaro, Renato²  Scocchi, Marco¹  Tossi, Alessandro¹  Skerlavaj, Barbara² 

[1] Dipartimento di Biochimica, Biofisica e Chimica delle Macromolecole, Università di Trieste, 34127 Trieste, Italy;Dipartimento di Scienze e Tecnologie Biomediche, Università di Udine, via Gervasutta 48, 33100 Udine, Italy

关键词: Antibacterial peptide;    CAP18;    Amphipathic helix;    Membrane permeabilization;    Leukocyte;   

DOI  :  10.1016/0014-5793(94)80395-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Secondary structure prediction studies on CAP18, a lipopolysaccharide binding protein from rabbit granulocytes, identified a highly cationic, 21-residue sequence with the tendency to adopt an amphipathic α-helical conformation, as observed in many antimicrobial peptides. The corresponding peptide was chemically synthesized and shown to exert a potent bacterieidal activity against both Gram-negative and Gram-positive bacteria, and a rapid permeabilization of the inner membrane of Escherichia coli. Five analogues were synthesized to elucidate structure/activity relationships. It was found that helix disruption virtually eliminates antibacterial activity, while the degree of amphipathicity and the presence of an aromatic residue greatly affect the kinetics of bacterial inner membrane permeabilization.

【 授权许可】

Unknown