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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

Authors 

Song Yub ShinMyung Kyu LeeKil Lyong KimKyung Soo Hahm

Publisher 

Wiley-Blackwell

Issue Date 

1997

Citation 

Journal of Peptide Research, vol. 50, no. 0, pp. 279-285

Keywords 

Hybrid peptidesantitumor activityhemolytic activityα-helicity

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.

ISSN 

1397-002X

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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