ISSN:
1573-3904
Keywords:
α-aminoisobutyric acid peptide
;
chirality
;
hydrophobicity
;
isovaline peptide
;
lipopeptaibol
;
membrane activity
;
peptide synthesis
;
trikoningin
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Summary We synthesized by solution-phase methods the naturally occurring, 10-amino acid residue lipopeptaibol antibiotics trikoningins KBI and KBII, and the [l-Iva1] KB analogue, in which the amino acid in position 1 is different, with the aim at investigating the effect of hydrophobicity and chirality in that position. A solution conformational analysis, using FT-IR absorption and CD techniques, indicated that all of the three decapeptides are predominantly helical in a membrane-mimetic environment. Permeability measurements showed an increase of the activity from the [Aib1] peptide to the more hydrophobic [Iva1] peptides. Conversely, the effect of a change in chirality, obtained by replacingd-Iva1 withl-Iva, turned out to be of minor significance.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02443556