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

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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
Author(s)
Song Yub Shin; Joo Hyun Kang; Dong Gun Lee; So Yun Jang; Moo Yeol Seo; Kil Lyong Kim; Kyung Soo Hahm
Bibliographic Citation
Bulletin of Korean Chemical Society, vol. 20, no. 9, pp. 1078-1084
Publication Year
1999
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
Publisher
Wiley
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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