Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides
✍ Scribed by SHIN, SONG YUB ;LEE, MYUNG KYU ;KIM, KIL LYONG ;HAHM, KYUNG-SOO
- Book ID
- 110893631
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 539 KB
- Volume
- 50
- Category
- Article
- ISSN
- 1397-002X
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## Abstract In order to elucidate the structure–antiviral activity relationship of cecropin A (1–8)‐magainin 2 (1–12) (termed CA‐MA) hybrid peptide, several analogues with amino acid substitutions were synthesized. In a previous study, it was shown that serine at position 16 in CA‐MA hybrid peptide
A 15-residue hybrid peptide ( KWKLFKKIGAVLKVL-amide) incorporating partial sequences of cecropin A and melittin causes the release of carboxyfluoresceine encapsulated in phosphatidylcholine liposomes. Succinylation of the amino groups in the N-terminus and lysine side chains inhibits the effect of t