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)-C 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.

The synthesis of thiazolyl‐7‐aminocephalosporanic acid, a pharmaceutical precursor of the β‐lactam antibiotic drug cefodizime, could be successfully realized in a continuous microstructured flow system. This was accomplished by changing the process window from batch, having a reaction temperature of 60 °C with a reaction time of 1 h, to a flow system at temperatures > 100 °C and reaction times of several minutes. The space‐time yield could be increased by a factor of 130.

As ingle high-affinity fatty acid binding site in the important human transport protein serum albumin (HSA) is identified and characterized using an NBD (7-nitrobenz-2oxa-1,3-diazol-4-yl)-C 12 fatty acid. This ligand exhibits a1 :1 binding stoichiometry in its HSA complex with high sitespecificity.The complex dissociation constant is determined by titration experiments as well as radioactive equilibrium dialysis.C ompetition experiments with the knownH SA-binding drugs warfarin and ibuprofen confirm the new binding site to be different from Sudlow-sites Ia nd II. These binding studies are extended to other albumin binders and fatty acid derivatives.F urthermore 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.