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Title 

Antibacterial activities of peptides designed as hybrids of antimicrobial peptides

Authors 

Song Yub ShinJoo Hyun KangMyung Kyu LeeKyung Soo Hahm

Publisher 

Springer Verlag (Germany)

Issue Date 

1996

Citation 

Journal of Biochemistry and Molecular Biology, vol. 29, no. 6, pp. 545-548

Keywords 

Antibacterial activityHemolytic activityHybrid peptides

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.

ISSN 

1225-8687

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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