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

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. Antitum...

Full description

Saved in:
Bibliographic Details
Published in:The journal of peptide research 1997-10, Vol.50 (4), p.279-285
Main Authors: SHIN, SONG YUB, LEE, MYUNG KYU, KIM, KIL LYONG, HAHM, KYUNG-SOO
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antimicrobial Cationic Peptides
Antineoplastic Agents - chemical synthesis
Antineoplastic Agents - chemistry
Antineoplastic Agents - pharmacology
antitumor activity
Cell Survival - drug effects
Circular Dichroism
Hemolysis - drug effects
hemolytic activity
Humans
Hybrid peptides
Magainins
Melitten - chemistry
Melitten - pharmacology
Molecular Sequence Data
Peptide Fragments - chemical synthesis
Peptide Fragments - chemistry
Peptide Fragments - pharmacology
Peptides - chemistry
Peptides - pharmacology
Protein Structure, Secondary
Structure-Activity Relationship
Tumor Cells, Cultured
Xenopus Proteins
α-helicity
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 mm sodium dodecyl sulfate solution was more closely correlated to hemolytic activity than antitumor activity.
ISSN:1397-002X
1399-3011
DOI:10.1111/j.1399-3011.1997.tb01469.x