Premium
Specific interaction between cyclophilin and cyclic peptides
Author(s) -
Gallo Pasquale,
Saviano Michele,
Rossi Filomena,
Pavone Vincenzo,
Pedone Carlo,
Ragone Raffaele,
Stiuso Paola,
Colonna Giovanni
Publication year - 1995
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360360303
Subject(s) - cyclophilin , chemistry , cyclophilin a , cis trans isomerases , fkbp , isomerase , peptidylprolyl isomerase , stereochemistry , derivative (finance) , isomerization , prolyl isomerase , biophysics , biochemistry , pin1 , enzyme , microbiology and biotechnology , gene , financial economics , economics , biology , catalysis
Cyclophilin A, a peptidyl‐prolyl cis–trans isomerase that catalyzes the otherwise slow isomerization of Xaa‐Pro imidic bond, specifically binds the immunosuppressant cyclosporin A. Herein we reportevidence 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 spectroscopies, evidencing no remarkable rearrangement of protein structure organization. The possibility that cyclolinopeptide A could act as a substitute of cyclosporin A in the immunosuppression modulation is also briefly discussed. © 1995 John Wiley & Sons, Inc.