An approach based on the combined use of saturation transfer difference (STD), Tr-NOESY and Inter-ligand NOEs for PHArmacophore Mapping (INPHARMA) NMR techniques and docking calculations is reported, for the first time, for mapping interactions and specific binding sites of caproleic acid (10:1 cis-9), oleic acid (18:1 cis-9), linoleic acid (18:2 cis-9,12) and linolenic (18:3, cis-9,12,15) free fatty acids (FFAs) with non-labeled serum albumin (BSA/HSA). Significant negative inter-ligand NOEs...
[NMR paper] Molecular recognition patterns between vitamin B12 and human serum albumin explored through STD-NMR and spectroscopic methods
Molecular recognition patterns between vitamin B12 and human serum albumin explored through STD-NMR and spectroscopic methods
Ligand-receptor molecular recognitionis the basis of biological process. The Saturation Transfer Difference-NMR (STD-NMR) technique has been recently used to gain qualitative and quantitative information about physiological interactions at atomic-resolution. The molecular recognition patterns between Vitamin B12 (VB12) and human serum albumin (HSA) were investigated by STD-NMR supplemented by other spectroscopies and molecular docking. STD-NMR delivered a complete...
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05-01-2021 10:35 PM
[NMR paper] The influence of fatty acids on metoprolol - human serum albumin interaction in low affinity binding sites: a multifactorial NMR approach.
The influence of fatty acids on metoprolol - human serum albumin interaction in low affinity binding sites: a multifactorial NMR approach.
Related Articles The influence of fatty acids on metoprolol - human serum albumin interaction in low affinity binding sites: a multifactorial NMR approach.
Protein Pept Lett. 2018 Jan 15;:
Authors: Szkudlarek A, Mogielnicki M, Pentak D, Ploch A, Maciazek-Jurczyk M
Abstract
The aim of the study was to evaluate the mechanism of interaction between metoprolol (MTP) and human serum albumin (HSA)...
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01-18-2018 12:41 PM
[NMR paper] NMR metabolomics profiling of blood plasma mimics shows that medium- and long-chain fatty acids differently release metabolites from human serum albumin.
NMR metabolomics profiling of blood plasma mimics shows that medium- and long-chain fatty acids differently release metabolites from human serum albumin.
Related Articles NMR metabolomics profiling of blood plasma mimics shows that medium- and long-chain fatty acids differently release metabolites from human serum albumin.
J Magn Reson. 2013 Dec 12;239C:34-43
Authors: Jupin M, Michiels PJ, Girard FC, Spraul M, Wijmenga SS
Abstract
Metabolite profiling by NMR of body fluids is increasingly used to successfully differentiate patients...
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01-01-2014 03:05 PM
[NMR paper] NMR Metabolomics Profiling of Blood Plasma Mimics shows that Medium- and Long-chain Fatty Acids Differently Release Metabolites from Human Serum Albumin
NMR Metabolomics Profiling of Blood Plasma Mimics shows that Medium- and Long-chain Fatty Acids Differently Release Metabolites from Human Serum Albumin
Publication date: Available online 12 December 2013
Source:Journal of Magnetic Resonance</br>
Author(s): M.D. Jupin , P.J. Michiels , F.C. Girard , M. Spraul , S.S. Wijmenga</br>
Metabolite profiling by NMR of body fluids is increasingly used to successfully differentiate patients from healthy individuals. Metabolites and their concentrations are direct reporters of body biochemistry. However, in blood plasma...
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12-12-2013 11:39 PM
[NMR paper] NMR identification of endogenous metabolites interacting with fatted and non-fatted human serum albumin in blood plasma: Fatty acids influence the HSA-metabolite interaction.
NMR identification of endogenous metabolites interacting with fatted and non-fatted human serum albumin in blood plasma: Fatty acids influence the HSA-metabolite interaction.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR identification of endogenous metabolites interacting with fatted and non-fatted human serum albumin in blood plasma: Fatty acids influence the HSA-metabolite interaction.
J Magn Reson. 2013 Jan 8;228C:81-94
Authors: Jupin M, Michiels PJ, Girard FC, Spraul M,...
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02-03-2013 10:19 AM
NMR Identification of Endogenous Metabolites interacting with Fatted and Non-Fatted Human Serum Albumin in Blood Plasma: Fatty Acids influence the HSA-Metabolite Interaction
NMR Identification of Endogenous Metabolites interacting with Fatted and Non-Fatted Human Serum Albumin in Blood Plasma: Fatty Acids influence the HSA-Metabolite Interaction
Available online 8 January 2013
Publication year: 2013
Source:Journal of Magnetic Resonance</br>
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Metabolites and their concentrations are direct reporters on body biochemistry. Thanks to technical developments metabolic profiling of body fluids, such as blood plasma, by for instance NMR has in the past decade become increasingly accurate enabling successful clinical diagnostics. Human Serum...
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01-09-2013 10:01 AM
[NMR paper] 13C NMR studies of the binding of medium-chain fatty acids to human serum albumin.
13C NMR studies of the binding of medium-chain fatty acids to human serum albumin.
Related Articles 13C NMR studies of the binding of medium-chain fatty acids to human serum albumin.
J Lipid Res. 1994 Mar;35(3):458-67
Authors: Kenyon MA, Hamilton JA
Binding of the medium-chain fatty acids (MCFA), octanoic (OCT) and decanoic (DEC) acid, to human serum albumin (HSA) has been studied by 13C NMR spectroscopy. NMR spectra at 35 degrees C showed an apparently homogeneous binding environment (a single, narrow resonance for the 13C-enriched carboxyl...
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08-22-2010 03:33 AM
[NMR paper] 13C NMR studies of the binding of medium-chain fatty acids to human serum albumin.
13C NMR studies of the binding of medium-chain fatty acids to human serum albumin.
Related Articles 13C NMR studies of the binding of medium-chain fatty acids to human serum albumin.
J Lipid Res. 1994 Mar;35(3):458-67
Authors: Kenyon MA, Hamilton JA
Binding of the medium-chain fatty acids (MCFA), octanoic (OCT) and decanoic (DEC) acid, to human serum albumin (HSA) has been studied by 13C NMR spectroscopy. NMR spectra at 35 degrees C showed an apparently homogeneous binding environment (a single, narrow resonance for the 13C-enriched carboxyl...