Fine Tuning the Inhibition Profile of Cyclosporine A by Derivatization of the MeBmt Residue. Issue 1 (7th December 2012)

• Record Type: Journal Article
• Authors: Prell, Erik; Kahlert, Viktoria; Rücknagel, Karl Peter; Malešević, Miroslav; Fischer, Gunter
• Is Part Of: Chembiochem. Volume 14:Issue 1(2013)
• Page Start: 63
• Page End: 65
• Publication Date: 2012-12-07
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201200621
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Unique respect:</bold> 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.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1p96pk63" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>