PubMed · 459059
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H R Dettelbach, D A Bennett. Furosemide compared with hydrochlorothiazide.. https://doi.org/10.1001/jama.1979.03300080012012
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A difference diffusion-based NMR technique and cold-spray ionization mass spectrometry were employed as a solution-based approach for identifying a ligand binding with a protein receptor. The difference diffusion-based NMR technique, called difference NOE-pumping, can directly detect the ligand interacting with a protein receptor. This technique uses a simple pulse sequence and the diffusion filter can easily be optimized. The cold-spray ionization mass spectrometry (CSI-MS), a variant of electrospray ionization mass spectrometry (ESI-MS) operating at low temperature, has been applied to detect the ligand-receptor complex. The efficiency of these techniques for identifying binding ligands is demonstrated with the human serum albumin (HSA)-drug system.
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The binding conformations of oxyphenbutazone (OXY), Nepsilon-dansyl-L-lysine (DNS-LYS), and furosemide (FU) to human serum albumin (HSA) have been investigated by molecular dynamics (MD) calculations and transferred nuclear Overhauser effect (TRNOE) measurements. We have combined distance information obtained from the Conformational Analyzer with Molecular Dynamics And Sampling (CAMDAS) calculation and experimental NOE spectroscopy measurements to determine a "binding conformation" for each drug which binds to site I of HSA. For OXY, only one conformer (conf9) among the conformer set generated by MD calculation satisfied the distance restraint conditions obtained from TRNOE measurements. For DNS-LYS and FU, 17 and 5 conformers satisfied distance restraint conditions, respectively. The structure of conf9 of OXY was taken as a "template" to choose binding conformers for DNS-LYS and FU. By fitting the "template" to the 17 conformers of DNS-LYS and 5 conformers of FU, we could efficiently obtain one binding conformer for DNS-LYS (conf144) and FU (conf26). It is suggested from the feature of the binding conformation that the three-dimensional location of a hydrophobic aromatic ring, alkyl chain, and electronegative functional group is important for binding to site I of HSA. This method, which combines MD calculations and NOE information, is thought to be effective for determining the binding conformation of drugs to HSA.