The understanding of the interaction between non-steroidal anti-inflammatory drugs and human serum albumin plays a fundamental role in the development of new drugs and new therapeutic strategies. Several studies have been performed, nevertheless, the interaction phenomena are still not fully understood. In this work, high-field solution Nuclear Magnetic Resonance (NMR) spectroscopy was applied to compare the strength of the interaction of diclofenac sodium salt, ketorolac tris salt and...
[NMR paper] NMR-Guided Repositioning of Non-Steroidal Anti-Inflammatory Drugs into Tight Junction Modulators
NMR-Guided Repositioning of Non-Steroidal Anti-Inflammatory Drugs into Tight Junction Modulators
Bioavailability is a major bottleneck in the clinical application of medium molecular weight therapeutics, including protein and peptide drugs. Paracellular transport of these molecules is hampered by intercellular tight junction (TJ) complexes. Therefore, safe chemical regulators for TJ loosening are desired. Here, we showed a potential application of select non-steroidal anti-inflammatory drugs (NSAIDs) as TJ modulators. Based on our previous observation that diclofenac and flufenamic acid......
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04-03-2021 10:01 PM
[NMR paper] Selective binding and dynamics of imidazole alkyl sulfate ionic liquids with human serum albumin and collagen - a detailed NMR investigation.
Selective binding and dynamics of imidazole alkyl sulfate ionic liquids with human serum albumin and collagen - a detailed NMR investigation.
Selective binding and dynamics of imidazole alkyl sulfate ionic liquids with human serum albumin and collagen - a detailed NMR investigation.
Phys Chem Chem Phys. 2018 Mar 21;:
Authors: Reddy RR, Shanmugam G, Madhan B, Phani Kumar BVN
Abstract
The interaction of ionic liquid (IL) with protein is now becoming important as it stabilizes the protein due to the selective cation-anion...
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03-22-2018 06:35 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] Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies.
Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies.
Arch Biochem Biophys. 2016 Sep 15;606:81-9
...
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05-24-2017 07:40 PM
[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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07-18-2014 01:02 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
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Biochim Biophys Acta. 2011 Jan;1808(1):498-507
Authors: Mishra VK, Palgunachari MN, Hudson JS, Shin R, Keenum TD, Krishna NR, Anantharamaiah GM
The surprising observation that a 10-residue class G(?) peptide from apolipoprotein J, apoJ, possesses...