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Characterizing Active Pharmaceutical Ingredient Binding to Human Serum Albumin by Spin‐Labeling and EPR Spectroscopy 下载免费PDF全文
Till Hauenschild Jörg Reichenwallner Dr. Volker Enkelmann Prof. Dr. Dariush Hinderberger 《Chemistry (Weinheim an der Bergstrasse, Germany)》2016,22(36):12825-12838
Drug binding to human serum albumin (HSA) has been characterized by a spin‐labeling and continuous‐wave (CW) EPR spectroscopic approach. Specifically, the contribution of functional groups (FGs) in a compound on its albumin‐binding capabilities is quantitatively described. Molecules from different drug classes are labeled with EPR‐active nitroxide radicals (spin‐labeled pharmaceuticals (SLPs)) and in a screening approach CW‐EPR spectroscopy is used to investigate HSA binding under physiological conditions and at varying ratios of SLP to protein. Spectral simulations of the CW‐EPR spectra allow extraction of association constants (KA) and the maximum number (n) of binding sites per protein. By comparison of data from 23 SLPs, the mechanisms of drug–protein association and the impact of chemical modifications at individual positions on drug uptake can be rationalized. Furthermore, new drug modifications with predictable protein binding tendency may be envisaged. 相似文献
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Takahiko Sato Hideki Masumoto Hisamitsu Nagase Hideaki Kito Miki Niikawa 《应用有机金属化学》1997,11(3):231-235
Various organotin compounds caused strong hemolysis of erythrocytes. To investigate the mechanism of hemolysis, spin-labeling techniques with electron spin resonance (ESR) spectroscopy were used and the relationship between hemolytic toxicity and signal intensity was investigated. Two kinds of spin-labeled stearic acid in which the para- magnetic center was located at different sites on the alkyl chain (5- and 12-doxyl-stearic acids; 5- and 12-NS) were used. It became clear that the decrease of ESR signal intensity was related to the hemolytic toxicity of the organotin compounds. © 1997 by John Wiley & Sons, Ltd. 相似文献
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Janez trancar Aleh Kavalenka Primo Ziherl David Stopar Marcus A. Hemminga 《Journal of magnetic resonance (San Diego, Calif. : 1997)》2009,197(2):245-248
Site-directed spin-labeling electron spin resonance (SDSL-ESR) is a promising tool for membrane protein structure determination. Here we propose a novel way to translate the local structural constraints gained by SDSL-ESR data into a low-resolution structure of a protein by simulating the restrictions of the local conformational spaces of the spin label attached at different protein sites along the primary structure of the membrane-embedded protein. We test the sensitivity of this approach for membrane-embedded M13 major coat protein decorated with a limited number of strategically placed spin labels employing high-throughput site-directed mutagenesis. We find a reasonably good agreement of the simulated and the experimental data taking a protein conformation close to the one determined by fluorescence resonance energy transfer analysis [P.V. Nazarov, R.B.M. Koehorst, W.L. Vos, V.V. Apanasovich, M.A. Hemminga, FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein, Biophys. J. 92 (2007) 1296–1305]. 相似文献
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