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Total synthesis and membrane modifying properties of the lipopeptaibol trikoningin KB II and its analogues with acyl chains of different length at the N‐ and C‐termini
Author(s) -
Piazza Claudia,
Formaggio Fernando,
Crisma Marco,
Toniolo Claudio,
Kamphuis Johan,
Kaptein Bernard,
Broxterman Quirinus B.
Publication year - 1999
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199902)5:2<96::aid-psc185>3.0.co;2-g
Subject(s) - residue (chemistry) , peptide , membrane , chemistry , stereochemistry , n terminus , amino acid , biochemistry , peptide sequence , gene
Trikoningin KB II, a ten‐amino acid residue lipopeptaibol blocked at the N‐terminus by the n ‐octanoyl group and at the C‐terminus by the 1,2‐amino alcohol l ‐leucinol, and extracted from the fungus Trichoderma koningii , exhibits membrane‐modifying properties. We have synthesized by solution‐phase methods trikoningin KB II and several analogues with acyl chains of different length at the N‐ and C‐termini. Permeability measurements showed that an appropriate length of the linear acyl chain is a more important characteristic for the onset of significant membrane‐modifying activity than its position in the peptide chain. Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd.