Structure-activity relationships of cecropin-like peptides and their interactions with phospholipid membrane

• Published in: BMB reports Vol. 46; no. 5; pp. 282 - 287
• Main Authors: Lee, E.J., Konkuk University,Seoul, Republic of Korea, Jeong, K.W., Konkuk University,Seoul, Republic of Korea, Lee, J.H., Konkuk University,Seoul, Republic of Korea, Shin, A.R., Konkuk University,Seoul, Republic of Korea, Kim, J.K., Konkuk University,Seoul, Republic of Korea, Lee, J.Y., Kyungpook National University, Daegu, Republic of Korea, Lee, D.G., Kyungpook National University, Daegu, Republic of Korea, Kim, Y.M., Konkuk University,Seoul, Republic of Korea
• Format: Journal Article
• Language: English
• Published: Korea (South) Korean Society for Biochemistry and Molecular Biology 01.05.2013; 생화학분자생물학회
• Subjects: Animals; Anti-Infective Agents - chemical synthesis; Anti-Infective Agents - chemistry; Anti-Infective Agents - pharmacology; Antimicrobial Cationic Peptides - chemical synthesis; Antimicrobial Cationic Peptides - chemistry; Antimicrobial Cationic Peptides - metabolism; Antimicrobial Cationic Peptides - pharmacology; Antimicrobial peptide; ANTIMICROBIAL PROPERTIES; Bacteria - drug effects; Cecropin A; Cecropin A,Papiliocin; Cell Line; Circular Dichroism; ESPECTROSCOPIA RMN; Fluorescence; Fungi - drug effects; Humans; Magnetic Resonance Spectroscopy; Membrane Lipids - chemistry; Membrane Lipids - metabolism; Models, Biological; NMR SPECTROSCOPY; Papiliocin; Peptides - chemistry; Peptides - metabolism; Phospholipids - chemistry; Phospholipids - metabolism; PROPIEDADES ANTIMICROBIANAS; PROPRIETE ANTIMICROBIENNE; SPECTROSCOPIE RMN; Structure; Structure-Activity Relationship; 화학
• ISSN: 1976-6696; 1976-670X
• DOI: 10.5483/BMBRep.2013.46.5.252

Cecropin A and papiliocin are novel 37-residue cecropin-like antimicrobial peptides isolated from insect. We have confirmed that papiliocin possess high bacterial cell selectivity and has an α-helical structure from Lys3 to Lys21 and from Ala25 to Val35, linked by a hinge region. In this study, we demonstrated that both peptides showed high antimicrobial activities against multi-drug resistant Gram negative bacteria as well as fungi. Interactions between these cecropin-like peptides and phospholipid membrane were studied using CD, dye leakage experiments, and NMR experiments, showing that both peptides have strong permeabilizing activities against bacterial cell membranes and fungal membranes as well as Trp2 and Phe5 at the N-terminal helix play an important role in attracting cecropin-like peptides to the negatively charged bacterial cell membrane. Cecropin-like peptides can be potent peptide antibiotics against multi-drug resistant Gram negative bacteria and fungi.