[NMR paper] Comparative analysis the binding affinity of mycophenolic sodium and meprednisone with human serum albumin: insight by NMR relaxation data and docking simulation.
Comparative analysis the binding affinity of mycophenolic sodium and meprednisone with human serum albumin: insight by NMR relaxation data and docking simulation.
Related ArticlesComparative analysis the binding affinity of mycophenolic sodium and meprednisone with human serum albumin: insight by NMR relaxation data and docking simulation.
Chem Biol Interact. 2016 Feb 15;
Authors: Ma X, He J, Yan J, Wang Q, Li H
Abstract
Mycophenolic sodium is an immunosuppressive agent that is always combined administration with corticosteroid in clinical practice. Considering the distribution and side-effect of the drug may change when co-administrated drug exist, this paper comparatively analyzed the binding ability of mycophenolic sodium and meprednisone toward human serum albumin by nuclear magnetic resonance relaxation data and docking simulation. The nuclear magnetic resonance approach was based on the analysis of proton selective and non-selective relaxation rate enhancement of the ligand in the absence and presence of macromolecules. The contribution of the bound ligand fraction to the observed relaxation rate in relation to protein concentration allowed the calculation of the affinity index. This approach allowed the comparison of the binding affinity of mycophenolic sodium and meprednisone. Molecular modeling was operated to simulate the binding model of ligand and albumin through Autodock 4.2.5. Competitive binding of mycophenolic sodium and meprednisone was further conducted through fluorescence spectroscopy.
PMID: 26892221 [PubMed - as supplied by publisher]
[NMR paper] Study of interaction of human serum albumin with curcumin by NMR and docking.
Study of interaction of human serum albumin with curcumin by NMR and docking.
Study of interaction of human serum albumin with curcumin by NMR and docking.
J Mol Model. 2014 Aug;20(8):2365
Authors: Singh DV, Bharti SK, Agarwal S, Roy R, Misra K
Abstract
Curcumin has been reported to be therapeutically active but has poor bioavailability, half life, and high rate of metabolic detoxifcation. Most of the hydrophobic and acidic drugs get transported through human serum albumin (HSA). Binding of drugs to serum protein increases their...
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[NMR paper] Mn(II) binding to human serum albumin: a ¹H-NMR relaxometric study.
Mn(II) binding to human serum albumin: a ¹H-NMR relaxometric study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Mn(II) binding to human serum albumin: a ¹H-NMR relaxometric study.
J Inorg Biochem. 2012 Dec;117:198-203
Authors: Fanali G, Cao Y, Ascenzi P, Fasano M
Abstract
Human serum albumin (HSA) displays several metal binding sites, participating to essential and toxic metal ions disposal and transport. The major Zn(II) binding site,...
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09-27-2013 03:28 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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[NMR paper] NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural di
NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural distortion upon amadori modification.
Related Articles NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural distortion upon amadori modification.
J Biol Chem. 2005 Jun 17;280(24):22582-9
Authors: Howard MJ, Smales CM
The non-enzymatic reaction between reducing sugars and long-lived proteins in vivo results in the formation of glycation and advanced glycation end products, which alter the properties of proteins including charge,...
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[NMR paper] Analysis of competitive binding of ligands to human serum albumin using NMR relaxatio
Analysis of competitive binding of ligands to human serum albumin using NMR relaxation measurements.
Related Articles Analysis of competitive binding of ligands to human serum albumin using NMR relaxation measurements.
J Pharm Biomed Anal. 2004 Feb 4;34(2):247-54
Authors: Cui YF, Bai GY, Li CG, Ye CH, Liu ML
The competitive binding of two ligands, ibuprofen (IBP) and salicylic acid (SAL), to human serum albumin (HSA) was studied by using nuclear magnetic resonance (NMR) relaxation measurements. When the concentration of one ligand was...
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11-24-2010 09:25 PM
[NMR paper] The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and
The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and 1H and 19F NMR investigation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and 1H and 19F NMR investigation.
J Pharm Biomed Anal. 1995 Aug;13(9):1087-93
Authors: Bertucci C, Ascoli G, Uccello-Barretta G, Di Bari L, Salvadori P
5-Fluorouracil (FU) is an important and widely used antineoplastic drug...
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[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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[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...
Comparative analysis the binding affinity of mycophenolic sodium and meprednisone with human serum albumin: insight by NMR relaxation data and docking simulation.
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