Fine tuning the inhibition profile of cyclosporine A by derivatization of the MeBmt residue

Erik Prell; Viktoria Kahlert; Karl Peter Rücknagel; Miroslav Malešević; Gunter Fischer

doi:10.1002/cbic.201200621

Fine tuning the inhibition profile of cyclosporine A by derivatization of the MeBmt residue

Chembiochem. 2013 Jan 2;14(1):63-5. doi: 10.1002/cbic.201200621. Epub 2012 Dec 7.

Authors

Erik Prell¹, Viktoria Kahlert, Karl Peter Rücknagel, Miroslav Malešević, Gunter Fischer

Affiliation

¹ Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale, Germany.

PMID: 23225707
DOI: 10.1002/cbic.201200621

Abstract

Unique respect: The biological properties of four CsA derivatives were fine-tuned by tractable modifications of the MeBmt residue. The new CsA derivatives share strong inhibitory activity toward cyclophilins (Cyps), but each is unique with respect to immunosuppressive action and cellular localization. These CsA analogues can be used to study the physiological roles of extracellular Cyps.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Biological Transport
Calcineurin Inhibitors
Cyclophilins / antagonists & inhibitors
Cyclosporine / chemistry*
Cyclosporine / metabolism
Cyclosporine / pharmacology*
Drug Design*
Enzyme Inhibitors / chemistry*
Enzyme Inhibitors / metabolism
Enzyme Inhibitors / pharmacology*
Extracellular Space / metabolism
Humans
Intracellular Space / metabolism
Jurkat Cells
Structure-Activity Relationship
Threonine / analogs & derivatives*
Threonine / chemistry*

Substances

Calcineurin Inhibitors
Enzyme Inhibitors
Threonine
Cyclosporine
Cyclophilins