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A Cyclosporin Derivative Discriminates between Extracellular and Intracellular Cyclophilins
Author(s) -
Malešević Miroslav,
Kühling Jan,
Erdmann Frank,
Balsley Molly A.,
Bukrinsky Michael I.,
Constant Stephanie L.,
Fischer Gunter
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200904529
Subject(s) - cypa , cyclophilin a , cyclophilin , extracellular , intracellular , oligopeptide , chemistry , rhodamine , biochemistry , microbiology and biotechnology , fluorescence , biophysics , computational biology , biology , peptide , physics , quantum mechanics , gene
Trimesic acid amide serves as a scaffold for a lipophilic cyclophilin inhibitor, a fluorescent rhodamine dye (TAMRA), and a ( D ‐Glu) 6 oligopeptide residue. Although the affinity of 1 for intracellular cyclophilin A (CypA) is very high, fluorescence measurements indicate complete exclusion from the cell. CypA‐induced chemotaxis of lymphocytes is inhibited by 1 since extracellular cyclophilins are responsible for the physiological signal.