Related ArticlesAllosteric Sensing of Fatty Acid Binding by NMR: Application to Human Serum Albumin.
J Med Chem. 2016 Aug 25;59(16):7457-65
Authors: Jafari N, Ahmed R, Gloyd M, Bloomfield J, Britz-McKibbin P, Melacini G
Abstract
Human serum albumin (HSA) serves not only as a physiological oncotic pressure regulator and a ligand carrier but also as a biomarker for pathologies ranging from ischemia to diabetes. Moreover, HSA is a biopharmaceutical with a growing repertoire of putative clinical applications from hypovolemia to Alzheimer's disease. A key determinant of the physiological, diagnostic, and therapeutic functions of HSA is the amount of long chain fatty acids (LCFAs) bound to HSA. Here, we propose to utilize (13)C-oleic acid for the NMR-based assessment of albumin-bound LCFA concentration (CONFA). (13)C-Oleic acid primes HSA for a LCFA-dependent allosteric transition that modulates the frequency separation between the two main (13)C NMR peaks of HSA-bound oleic acid (??AB). On the basis of ??AB, the overall [(12)C-LCFA]Tot/[HSA]Tot ratio is reproducibly estimated in a manner that is only minimally sensitive to glycation, albumin concentration, or redox potential, unlike other methods to quantify HSA-bound LCFAs such as the albumin-cobalt binding assay.
[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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[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 reveals molecular interactions and dynamics of fatty acid binding to albumin.
NMR reveals molecular interactions and dynamics of fatty acid binding to albumin.
NMR reveals molecular interactions and dynamics of fatty acid binding to albumin.
Biochim Biophys Acta. 2013 Aug 9;
Authors: Hamilton JA
Abstract
BACKGROUND: The molecular details of fatty acid (FA) interactions with albumin are fundamental to understanding transport in the plasma and cellular utilization of these key nutrients and building blocks of membranes.
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08-14-2013 05:24 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
DEER in Biological Multispin-Systems: A Case Study on the Fatty Acid Binding to Human Serum Albumin
DEER in Biological Multispin-Systems: A Case Study on the Fatty Acid Binding to Human Serum Albumin
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 10 March 2011</br>
Matthias J.N., Junk , Hans W., Spiess , Dariush, Hinderberger</br>
In this study, self-assembled systems of human serum albumin (HSA) and spin-labeled fatty acids are characterized by double electron–electron resonance (DEER). HSA, being the most important transport protein of the human blood, is capable to host up to seven paramagnetic fatty acid...
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03-11-2011 05:00 PM
[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...
Allosteric Sensing of Fatty Acid Binding by NMR: Application to Human Serum Albumin.
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