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Title 

Influences of hinge region of a synthetic antimicrobial peptide, cecropin A(1-13)-Melittin(1-13) hybrid on antibiotic activity

Authors 

Song Yub ShinJoo Hyun KangDong Gun LeeSo Yun JangMoo Yeol SeoKil Lyong KimKyung Soo Hahm

Publisher 

The Korean Chemical Society

Issue Date 

1999

Citation 

Bulletin of the Korean Chemical Society, vol. 20, no. 9, pp. 1078-1084

Keywords 

antiinfective agentcecropin a[1-13] melittin[1-13]hybrid proteinunclassified drugantifungal activityantimicrobial activityantineoplastic activitybacterial growthhannel gatinghuman

Abstract 

A synthetic cecropin A(1-13)-melittin(1-13) [CA-ME] hybrid peptide was known to be an antimicrobial peptide having strong antibacterial, antifungal and antitumor activity with minimal cytotoxic effect against human erythrocyte. Analogues were synthesized to investigate the influences of the flexible hinge region of CA-ME on the antibiotic activity. Antibiotic activity of the peptides was measured by the growth inhibition against bacterial, fungal and tumor cells and vesicle-aggregating or disrupting activity. The deletion of Gln-Gly-Ile (P1) or Gly-Gln-Gly-Ile-Gly (P3) from CA-ME brought about a significant decrease on the antibiotic activities. In contrast, Gly-Ile-Gly deletion (P2) from CA-ME or Pro insertion (P5) instead of Gly-Gln-Gly-Ile-Gly of CA-ME retained antibiotic activity. This result indicated that the flexible hinge or β-bend structure provided by Gly-Gln- Gly-Ile-Gly, Gln-Gly, or Pro in the central region of the peptides is requisite for its effective antibiotic activity and may facilitate easily the hydrophobic C-terminal region of the peptide to penetrate the lipid bilayers of the target cell membrane. In contrast, P4 and P6 with Gly-Gln-Gly-Pro-Gly or Gly-Gln-Pro in the central region of the peptide caused a drastic reduction on the antibiotic activities. This result suggested that the consecutive β-bend structure provided by Gly-Gln-Gly-Pro-Gly or Gly-Gln-Pro in the central hinge region of the peptide seems to interrupt the ion channel/pore formation on the target cell membranes.

ISSN 

0253-2964

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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