Related ArticlesAnalysis 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 increased in the solution containing IBP, SAL and HSA, the fractions of free IBP and SAL were increased because of the competitive binding. The 1H relaxation rates (R1) of both ligands were subsequently decreased. If a ligand is in fast exchanging between the free and bound forms, the observed 1H relaxation rate is a weighted average of that for the free ligand and the protein-ligand complex. The concentrations of the free and bound ligands can be quantitatively derived from the relaxation rates. The results presented in this work revealed that IBP and SAL shared certain low-affinity binding sites on the HSA molecule, in addition to the same high-affinity binding site of AIII.
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] Epitope mapping and competitive binding of HSA drug site II ligands by NMR diffusion
Epitope mapping and competitive binding of HSA drug site II ligands by NMR diffusion measurements.
Related Articles Epitope mapping and competitive binding of HSA drug site II ligands by NMR diffusion measurements.
J Am Chem Soc. 2004 Nov 3;126(43):14258-66
Authors: Lucas LH, Price KE, Larive CK
It is important to characterize drug-albumin binding during drug discovery and lead optimization as strong binding may reduce bioavailability and/or increase the drug's in vivo half-life. Despite knowing about the location of human serum albumin (HSA)...
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[NMR paper] Direct binding of ethanol to bovine serum albumin: a fluorescent and 13C NMR multiple
Direct binding of ethanol to bovine serum albumin: a fluorescent and 13C NMR multiplet relaxation study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Direct binding of ethanol to bovine serum albumin: a fluorescent and 13C NMR multiplet relaxation study.
Biochemistry. 1996 Jan 9;35(1):340-7
Authors: Avdulov NA, Chochina SV, Daragan VA, Schroeder F, Mayo KH, Wood WG
Molecular mechanisms of ethanol interaction with proteins are not well-understood. In the present study, direct...
[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...
Analysis of competitive binding of ligands to human serum albumin using NMR relaxatio
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