Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides

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Title
Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides
Author(s)
Song Yub Shin; Myung Kyu Lee; Kil Lyong Kim; Kyung Soo Hahm
Bibliographic Citation
Chemical Biology & Drug Design, vol. 50, pp. 279-285
Publication Year
1997
Abstract
The hybrid peptide (CA-ME) derived from cecropin A(1-8) and melittin(1- 12) has potent antibacterial and antimalarial activities. Because the N- terminal sequence 1-12 of magainin 2 is similar to melittin(1-12), CA-MA with CA(1-8) and MA(1-12) and their analogues were designed and synthesized. Antitumor activities of these peptides were evaluated using three small cell lung cancer cell lines. Greater antitumor activity was observed when the residues 16, 18 and 19 of the peptide were hydrophobic (Leu or Val), basic (Lys) and basic (Lys), respectively. The IC50 values of the peptides with the residues were 2 to 4 μM. Residue 12 was related to hemolytic activity rather than antitumor activity. Increase in amphipathicity of P4 enhanced hemolytic activity without significant change in antitumor activity. The α- helicity of the peptides in a 30 nm sodium dodecyl sulfate solution was more closely correlated to hemolytic activity than antitumor activity.
Keyword
Hybrid peptidesantitumor activityhemolytic activityα-helicity
ISSN
1397-002X
Publisher
Wiley
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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