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Title 

Effects of the hinge region of cecropin A(1-8)-melittin 2(1-12), a synthetic antimicrobial peptide on antibacterial, antitumor, and vesicle-disrupting activity

Authors 

Song Yup ShinJoo Hyun KangSo Yun JangKil Lyong KimKyung Soo Hahm

Publisher 

Springer Verlag (Germany)

Issue Date 

1999

Citation 

Journal of Biochemistry and Molecular Biology, vol. 32, no. 6, pp. 561-566

Keywords 

Antitumor activityCA(1-8)-ME(1-12)Helix-hinge-helix structureHinge regionVesicle-disrupting activity

Abstract 

CA(1-8)-ME(1-12) [CA-ME], composed of cecropin A(1-8) and melittin(1-12), is a synthetic antimicrobial peptide having potent antibacterial and antitumor activities with minimal hemolytic activity. In order to investigate the effects of the flexible hinge sequence, Gly-Ile-Gly, of CA-ME on antibiotic activity, CA-ME and three analogues, CA-ME1, CA-ME2, and CA-ME3, were synthesized. The Gly-Ile-Gly sequence of CA-ME was deleted in CA-ME1 and replaced with Pro and Gly-Pro-Gly in CA-ME2 and CA-ME3, respectively. CA-ME1 and CA-ME3 showed a significant decrease in antitumor activity and phospholipid vesicle-disrupting ability. However, CA-ME2 showed similar antitumor and vesicle-disrupting activities, as compared with CA-ME. These results suggest that the flexibility or β-turn induced by Gly-Ile-Gly or Pro in the central part of CA-ME may be important in the electrostatic interaction of the N-terminus cationic α-helical region with the cell membrane surface and the hydrophobic interaction of the C-terminus amphipathic α-helical region with the hydrophobic acyl chains in the cell membrane. CA-ME3 exhibited lower antitumor and vesicle-disrupting activities than CA-ME and CA-ME2. This result suggests that the excessive β-turn structure caused by the Gly-Pro-Gly sequence in CA-ME3 seems to interrupt ion channel/pore formation in the lipid bilayer. We concluded that the appropriate flexibility or β-turn structure provided by the central hinge is responsible for the effective antibiotic activity of the antimicrobial peptides with the helix-hinge-helix structure.

ISSN 

1225-8687

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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