α-aminoisobutyric acid peptide
Springer Online Journal Archives 1860-2000
Chemistry and Pharmacology
Abstract We synthesized by solution-phase methods thenaturally occurring, 10-amino acid residuelipopeptaibol antibiotics trikoningins KBI and KBII,and the [L-Iva1] KB analogue, in which the aminoacid in position 1 is different, with the aim atinvestigating the effect of hydrophobicity andchirality in that position. A solution conformationalanalysis, using FT–IR absorption and CD techniques,indicated that all of the three decapeptides arepredominantly helical in a membrane-mimeticenvironment. Permeability measurements showed anincrease of the activity from the [Aib1] peptideto the more hydrophobic [Iva1] peptides.Conversely, the effect of a change in chirality,obtained by replacing D-Iva1 with L-Iva, turnedout to be of minor significance.
Type of Medium: