Effects on electrophoretic mobility and antibacterial spectrum of removal of two residues from synthetic sarcotoxin IA and addition of the same residues to cecropin B

FEBS Letters

Boman, Hans G.²  Merrifield, R.B.¹  Li, Zong-qu¹  Boman, I.Anita² 

[1] The Rockefeller University, New York, NY 10021, USA;Department of Microbiology, University of Stockholm, S-106 91 Stockholm, Sweden

关键词: Cecropin B;    Sarcotoxin IA;    Solid-phase synthesis;    C-terminal amide effect;    Antibacterial peptide;    Insect immunity;   

DOI  :  10.1016/0014-5793(88)80837-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cecropin B and cecropin IA (sarcotoxin IA) are 35- and 39-residue antibacterial peptides from a silk moth and a meat fly, respectively. Using solid phase synthesis we have made these peptides as well as two 37-residue analogs, one containing a deletion of leucine and lysine (residues 2a and 2b) as compared to cecropin IA, the other containing an insertion of leusine and lysine at the corresponding place in cecropin B. This addition and removal of a lysine residue did not cause the expected change in electrophoretic mobility. When tested for antibacterial spectra, the insertion analog was found to be as active as the parent compound while the deletion analog had lost most of its antibacterial capacity. In addition it was shown that the C-terminal amide contributes to the broad spectrum properties of the cecropins.

【 授权许可】

Unknown