Antibacterial activities of peptides designed as hybrids of antimicrobial peptides

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Title
Antibacterial activities of peptides designed as hybrids of antimicrobial peptides
Author(s)
Song Yub Shin; Joo Hyun Kang; Myung Kyu Lee; Kyung Soo Hahm
Bibliographic Citation
BMB Reports, vol. 29, no. 6, pp. 545-548
Publication Year
1996
Abstract
CA(1-8)ME(1-12), the CA-ME hybrid peptide of the amino terminal segments of cecropin A (CA) and melittin (ME), has been reported to have a broad spectrum and improved potency without a hemolytic property. In order to obtain new synthetic peptides with powerful antibacterial activity without hemolytic activity, several hybrid peptides were designed from the sequences of CA. ME, magainin 2, bombinin and lactofenricin. All hybrid peptides were constructed to form an amphipathically basic-flexible-hydrophobic structure and synthesized by the solid phase method. Their hemolytic activities against human red blood cells and antibacterial activities against both Gram-positive and Gram-negative bacteria were determined. CA(1-8)MA(1-12). CA(1-8)BO(1-12). MA(10-17)ME(1-12) and LF(20-29)ME(1-12) showed comparable activities with broad spectra against both Gram-positive and Gram-negative bacteria relative to CA(1-8)ME(1-12) but without hemolytic properties. These hybrid peptides, therefore, could be useful as model peptides to design a novel peptide with improved antibacterial activity and study on structure-activity relationships of antimicrobial peptides.
Keyword
Antibacterial activityHemolytic activityHybrid peptides
ISSN
1225-8687
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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