NMR Study on the Low-Affinity Interaction of Human Serum Albumin with Diclofenac Sodium.

Ji, Zhusheng; Li, Conggang; Mao, Xi‐an; Liu, Maili; Hu, Jiming

doi:10.1248/cpb.50.1017

Cited by 25 publications

(9 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, the presence of two aromatic rings in Diclofenac might confer a hydrophobic character to this interaction whereby the aromatic moieties interact with Sudlow's site II of BSA and the carboxylate group moiety with charged amino-acid residues in or around the hydrophobic cavity as reported in several crystallographic studies [11,24,27]. Our ITC data is also consistent with earlier studies suggesting that Diclofenac can interact with the protein via ionic and hydrophobic interactions [28][29][30][31].…”

Section: Itc Of Diclofenac and Naproxen Binding To Bsasupporting

confidence: 91%

Binding thermodynamics of Diclofenac and Naproxen with human and bovine serum albumins: A calorimetric and spectroscopic study

Bou-Abdallah

Sprague

Smith

et al. 2016

The Journal of Chemical Thermodynamics

View full text Add to dashboard Cite

Serum albumins are ubiquitous proteins able to bind a variety of exogenous and endogenous ligands including hydrophobic pharmaceuticals. Most drugs bind to two very active binding regions located within sub-domains IIA and IIIA of the protein, also known as Sudlow's sites. The drug binding mode of serum albumin provides important pharmacological information and influences drug solubility, efficacy, biological distribution, and excretion. Here, the binding thermodynamics of Diclofenac and Naproxen, two non-steroidal anti-inflammatory drugs (NSAIDs) to bovine and human serum albumins (BSA and HSA, respectively) were studied by isothermal titration calorimetry (ITC), fluorescence spectroscopy and differential scanning calorimetry (DSC). The ITC data show that the binding affinity (K) of Diclofenac to BSA and HSA is on the order of 10 4 M-1 with a binding stoichiometry (n) of 2 drug molecules per protein. Naproxen binding to the two proteins exhibits a different profile with K and n values on the order of 10 6 M-1 and 0.75 for BSA and 10 5 M-1 and 3 for HSA, respectively. The binding of the two drugs to HSA is found to be both enthalpically and entropically favored suggesting the formation of hydrogen bonds and van der Waals hydrophobic effects. Binding of the two drugs to BSA is only enthalpically favored with an unfavorable entropy term. Significant enthalpyentropy compensation phenomena were reported for Diclofenac and Naproxen binding to BSA but not to HSA. Fluorescence quenching data between Diclofenac and the two proteins suggest static collisions and the formation of ground-state protein-drug complexes. The DSC data corroborate the ITC findings and show multiple sequential unfolding events and a strong drug stabilization effect at high drug to protein ratios. Overall, the calorimetric and spectroscopic data provided insights into the nature of these protein-drugs interactions and might offer useful information in future drug discovery studies.

show abstract

Section: Itc Of Diclofenac and Naproxen Binding To Bsasupporting

confidence: 91%

Binding thermodynamics of Diclofenac and Naproxen with human and bovine serum albumins: A calorimetric and spectroscopic study

Bou-Abdallah

Sprague

Smith

et al. 2016

The Journal of Chemical Thermodynamics

View full text Add to dashboard Cite

show abstract

“…There are numerous methods applicable for study on drug binding to plasma proteins [1][2][3][4][5]. Current high performance capillary electrophoresis (CE) is one of the most dynamically growing analytical techniques in studying molecular interactions because of its speed, efficiency, and selectivity.…”

Section: Introductionmentioning

confidence: 99%

Protein binding study of clozapine by capillary electrophoresis in the frontal analysis mode

Zhou

2004

Journal of Pharmaceutical and Biomedical Analysis

View full text Add to dashboard Cite

“…B, C, D and F). These spectral transitions would be highly indicative of protein binding with these chemicals, and the observations were partly in agreement with previous reports on potent serum protein‐binding properties of these chemicals (Gulden et al ., ; Ji et al ., ). Although the aROS assay demonstrated the considerable changes in photochemical properties of quinine HCl ( 1 ) and lomefloxacin HCl ( 15 ) in the presence of serum albumin, no spectral differences were observed in these chemicals with or without serum albumin (Fig.…”

Section: Resultsmentioning

confidence: 99%

Development of an albuminous reactive oxygen species assay for photosafety evaluation under experimental biomimetic conditions

Onoue

Kato

Yamada

2013

J of Applied Toxicology

View full text Add to dashboard Cite

The generation of reactive oxygen species (ROS) from an ultraviolet (UV)-exposed chemical can be an experimental indicator of phototoxic potential. The aim of the present study was to develop a new ROS assay using serum albumin to provide photosafety assessment under experimental biomimetic conditions. To assess assay robustness, a validation study on an albuminous ROS (aROS) assay was conducted with a focus on intra- and inter-day precisions and Z'-factor reflecting both the assay signal-to-noise ratio and variation associated with signal measurements. In the aROS assay on quinine HCl (200 μM), a typical phototoxic drug, both intra- and inter-day precisions (coefficient of variation; CV) were found to be below 4%, and the Z'-factors for singlet oxygen and superoxide suggested a large separation band between samples and blank signals. To evaluate the prediction capacity, the aROS and ROS assays were applied to 21 phototoxins and 10 non-phototoxic chemicals. Upon aROS assay on these model chemicals, the individual specificity was 100%, and the positive and negative predictivities were found to be 100% and 81.8%, respectively. The aROS assay can be employed for poorly soluble chemicals for which the ROS assay is unavailable. Comparing the ROS assay data, there seemed to be a photochemical transition of some chemicals in albuminous solution. A molecular interaction between albumin and chemical was also assessed by UV and fluorescent spectroscopic analyses, and the results suggested the limited relationship between the albumin-chemical interaction and the photochemical change. The aROS assay may allow photosafety assessment of new drug entities with a wide range of applicability partly under experimental biomimetic conditions.

show abstract

NMR Study on the Low-Affinity Interaction of Human Serum Albumin with Diclofenac Sodium.

Abstract: The low-affinity interaction between human serum albumin (HSA) and Diclofenac sodium (DCF) was studied using NMR techniques. Both

Cited by 25 publications

References 25 publications

Binding thermodynamics of Diclofenac and Naproxen with human and bovine serum albumins: A calorimetric and spectroscopic study

Binding thermodynamics of Diclofenac and Naproxen with human and bovine serum albumins: A calorimetric and spectroscopic study

Protein binding study of clozapine by capillary electrophoresis in the frontal analysis mode

Development of an albuminous reactive oxygen species assay for photosafety evaluation under experimental biomimetic conditions

Contact Info

Product

Resources

About