96801-39-7Relevant articles and documents
Identification and Characterization of a Single High-Affinity Fatty Acid Binding Site in Human Serum Albumin
Wenskowsky, Lea,Schreuder, Herman,Derdau, Volker,Matter, Hans,Volkmar, Julia,Nazaré, Marc,Opatz, Till,Petry, Stefan
supporting information, p. 1044 - 1048 (2018/01/01)
A single high-affinity fatty acid binding site in the important human transport protein serum albumin (HSA) is identified and characterized using an NBD (7-nitrobenz-2-oxa-1,3-diazol-4-yl)-C12 fatty acid. This ligand exhibits a 1:1 binding stoichiometry in its HSA complex with high site-specificity. The complex dissociation constant is determined by titration experiments as well as radioactive equilibrium dialysis. Competition experiments with the known HSA-binding drugs warfarin and ibuprofen confirm the new binding site to be different from Sudlow-sites I and II. These binding studies are extended to other albumin binders and fatty acid derivatives. Furthermore an X-ray crystal structure allows locating the binding site in HSA subdomain IIA. The knowledge about this novel HSA site will be important for drug depot development and for understanding drug-protein interaction, which are important prerequisites for modulation of drug pharmacokinetics.
Development of a novel FRET probe for the real-time determination of ceramidase activity
Bhabak, Krishna P.,Hauser, Anett,Redmer, Susanne,Banhart, Sebastian,Heuer, Dagmar,Arenz, Christoph
, p. 1049 - 1052 (2013/07/26)
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Novel fluorescent ceramide derivatives for probing ceramidase substrate specificity
Bhabak, Krishna P.,Proksch, Denny,Redmer, Susanne,Arenz, Christoph
, p. 6154 - 6161 (2012/11/07)
Ceramidases are key regulators of cell fate. The biochemistry of different ceramidases and of their substrate ceramide appears to be complex, mainly due to specific biophysical characteristics at the water-membrane interface. In the present study, we describe the design and synthesis of a set of fluorescently labeled ceramides as substrates for acid and neutral ceramidases. For the first time we have replaced the commonly used polar NBD-dye with the lipophilic Nile Red (NR) dye. Analysis of kinetic data reveal that although both the dyes do not have any noticeable preference for the substitution at acyl or sphingosine (Sph) part in ceramide towards hydrolysis by acid ceramidase, the ceramides with acyl-substituted NBD and Sph-substituted NR dyes have been found to be a better substrate for neutral ceramidase.