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Effect of succinylation on the membrane activity and conformation of a short cecropin A‐melittin hybrid peptide
Author(s) -
Fernández Imma,
Ubach Josep,
Reig Francesca,
Andreu David,
Pons Miquel
Publication year - 1994
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360340913
Subject(s) - melittin , succinylation , chemistry , peptide , magainin , liposome , phosphatidylcholine , peptide conformation , amphiphile , circular dichroism , residue (chemistry) , mastoparan , lysine , membrane , biochemistry , biophysics , stereochemistry , phospholipid , amino acid , antimicrobial peptides , organic chemistry , copolymer , biology , polymer , receptor , g protein
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 this peptide on liposome permeability. Conformational analysis of the parent peptide and its succinyl derivative by CD and nmr indicates that both peptides form amphipathic α‐helices in the presence of hexafluoro‐2‐propanol, but only the unmodified peptide acquires a relevant level of α‐helical conformation in the presence of liposomes. © 1994 John Wiley & Sons, Inc.