ISSN:
1573-3904
Schlagwort(e):
α-aminoisobutyric acid peptide
;
chirality
;
hydrophobicity
;
isovaline peptide
;
lipopeptaibol
;
membrane activity
;
peptide synthesis
;
trikoningin
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Chemie und Pharmazie
Notizen:
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.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1023/A:1008934505586
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