par De Coen, Jean-Louis ;Wathelet, Bernard;Demeuse, F.;Mayon, Catherine ;Culot, Marc;Brakel, J.
Référence International Journal of Peptide and Protein Research, 43, 1, page (10-18)
Publication Publié, 1994
Référence International Journal of Peptide and Protein Research, 43, 1, page (10-18)
Publication Publié, 1994
Article révisé par les pairs
Résumé : | A detailed theoretical conformational analysis of the linear heptapeptide antibiotic [Arg2]K-582 A (Arg-Arg-D-Orn-Thr-D-Orn-Lys-D-Tyr) was carried out. The results of the computer simulation suggest that the linear peptide has a high propensity to fold in solution into a quasi-cyclic conformation in equilibrium with π(L-D) helices. The synthesis of two inactive analogues with an L-Lys in place of D-Orn3 or D-Orn5 confirms the importance of the proposed folding pattern for the occurence of the antimicrobial activity of K-582 A. |