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

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 alc ohol L-leucinol, and extracted from the fungus Trichoderma koningii, exhibi ts membrane-modifying properties. We have synthesized by solution-phase met hods trikoningin KB II and several analogues with acyl chains of different length at the N- and C-termini. Permeability measurements showed that an ap propriate length of the linear acyl chain is a more important characteristi c for the onset of significant membrane-modifying activity than its positio n in the peptide chain. Copyright (C) 1999 European Peptide Society and Joh n Wiley gr Sons, Ltd.