Cyclophilin A, a peptidyl-prolyl cis-trans isomerase that catalyzes th
e otherwise slow isomerization of Xaa-Pro imidic bond, specifically, b
inds the immunosuppressant cyclosporin A. Herein we repel evidence on
binding of cyclolinopeptide A and its synthetic analogue, [Aib(5,6)-D-
Ala(8)] cyclolinopeptide, to bovine cyclophilin A. Binding experiments
were monitored by fluorescence, CD, and second-derivative spectroscop
ies, evidencing no remarkable rearrangement of protein structure organ
ization. The possibility, that cyclolinopeptide A could act as a subst
itute of cyclosporin A in the immunosuppression modulation is also bri
efly discussed. (C) 1995 John Wiley and Sons, Inc.