Albumin binding sites for etodolac enantiomers

Mignot, Isabelle; Presle, Nathalie; Lapicque, Françoise; Monot, C.; Dropsy, R.; Netter, Patrick

doi:10.1002/(sici)1520-636x(1996)8:3<271::aid-chir7>3.0.co;2-k

Cited by 35 publications

(20 citation statements)

References 31 publications

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“…17) In the present study, the unbound fraction of the R-enantiomer of warfarin increased with the increased length of the alcohol aliphatic chain. However, such characteristics on the binding of the S-enantiomer were not observed.…”

Section: Discussionsupporting

confidence: 52%

Effect of Ethanol on the Binding of Warfarin Enantiomers to Human Serum Albumin

Tatsumi

Kadobayashi

Iwakawa

2007

Biological & Pharmaceutical Bulletin

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Ethanol is widely used as a pharmaceutical excipient for the solubilization of many hydrophobic drugs for injections. However, there are only few studies about drug interaction with pharmaceutical excipients in the body after injection. In this study, the effect of ethanol (500 mM) or several alcohols (500 mM) on the stereoselective binding of warfarin enantiomers to fatty acid-free human serum albumin (HSA) or proteins of commercial albumin preparations was investigated. An ultrafiltration method was used for the separation of unbound warfarin enantiomers. By the addition of ethanol or 1-propanol, the unbound fraction of the S-enantiomer was decreased. On the other hand, the unbound fraction of the R-enantiomer was increased by the addition of ethanol or 1-propanol. Unbound fractions of both the S-and R-enantiomer were decreased by 2-propanol. In various commercial albumin preparations, unbound fractions of both the S-and R-enantiomer were increased by ethanol. The different effects of ethanol among fatty acid-free HSA and commercial albumin preparations were observed.

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Section: Discussionsupporting

confidence: 52%

Effect of Ethanol on the Binding of Warfarin Enantiomers to Human Serum Albumin

Tatsumi

Kadobayashi

Iwakawa

2007

Biological & Pharmaceutical Bulletin

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“…Drugs: Warfarin 1) 3.4ϫ10 5 10) Diazepam 1) 3.8ϫ10 5 48) Azapropazone 120) 2.8ϫ10 5 9) Ketoprofen 133) 2.5ϫ10 6 136) Phenylbutazone 1) 1.5ϫ10 6 10) Chlofibrate 1) 7.6ϫ10 5 137) Acenocoumarol 10) 2.2ϫ10 5 10) Iopanoate 1) 6.7ϫ10 6 131) Salicylate 1) 1.9ϫ10 5 9) Ibuprofen 22,68) 2.7ϫ10 6 21) Indomethacin 1) 1.4ϫ10 6 129) Pirprofen 72) 3.9ϫ10 5 72) Tolbutamide 1) 4.0ϫ10 4 130) S-Naproxen 1) 3.7ϫ10 6 89) Chlorpropamide 1) 3.3ϫ10 5 9) Ethacrynate 1) 1.7ϫ10 6 34) Iophenoxate 1) 7.7ϫ10 7 131) Chlorothiazide 134) 5.5ϫ10 4 134) Iodipamide 10) 9.9ϫ10 6 10) Diclofenac 76) 3.3ϫ10 6 76) Sulfadimethoxine 121) 9.0ϫ10 4 121) S(Ϫ)-Thiamylal 56) 8.7ϫ10 4 56) Sulfathiazole 9) 2.5ϫ10 4 9) S-Etodolac 59) 2.0ϫ10 5 59) Furosemide 122) 1.9ϫ10 5 122) Carprofen 75) Ͼ10 6 75) Tenoxicam 123) 3.7ϫ10 5 123) Suprofen 68) N.D. R-Sulbenicillin 111) 5.2ϫ10 3 111) Benoxaprofen 22) N.D. Valproate 60) 2.8ϫ10 5 60) Cicloprofen 22) N.D. Piretanide 122) 9.5ϫ10 4 122) Azidodeoxythymidine 15) N.D. Spironolactone …”

Section: Ligand Bindingunclassified

“…In contrast, the toxin has no effect on warfarin binding. 69) Chloride ions diminish the binding of warfarin, 70) tolmetin, 71) pirprofen, 72) etodolac, 59) azosemide, 73) bilirubin, 74) and perhaps other ligands as well. The displacing effect of chloride ions is also relevant for in vitro binding studies, because some widely used buffers contain a high concentration of chloride ions (for example in the form of 0.9% NaCl), whereas other buffers lack the ion.…”

Section: -3 Endogenous Compoundsmentioning

confidence: 99%

Practical Aspects of the Ligand-Binding and Enzymatic Properties of Human Serum Albumin.

Kragh‐Hansen

Chuang

Otagiri

2002

Biological & Pharmaceutical Bulletin

935

776

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Recent work with approaches like recombinant mutants and X-ray crystallography has given much new information about the ligand-binding properties of human serum albumin (HSA). The information increases the understanding of this unique transport and depot protein and could give a structural basis for the possible construction of therapeutic agents with altered HSA-binding properties. A tabulation of high-affinity binding sites for both endogenous and exogenous compounds has been made; it could be useful for the above-mentioned purpose, but it could also be of value when trying to predict potential drug interactions at the protein-binding level. Drug displacement is not always a complication to therapy; it can be used to increase the biological effect of a drug. However, due to rebinding at other sites, the increase in the free concentration of a displaced ligand can be less than expected. Drugs and drug metabolites can also interact covalently with HSA; thiol-containing drugs often bind to the single free cysteine residue of HSA, and glucuronidated drugs react irreversibly with other residues of the protein. Reversible binding of ligands is often stereospecific, and therefore immobilized HSA can be used to separate drug isomers. Albumin-containing dialysates are useful for extracorporeal removal of endogenous toxins and in the treatment of drug overdoses. HSA has different types of hydrolytic activities, which also can be stereospecific. The esterase-like property seems especially useful in converting prodrugs to active drugs in plasma.

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“…24) The displacement probes were bilirubin 23) and ketoprofen 25) for site I, ibuprofen 23) and chlorphenamine maleate 26) for site II. The percentage of displacement of the probe was determined according to the method of Sudlow et al 27) probe displacement (%)ϭF 2 /F 1 ϫ100 (5) where F 1 and F 2 represent the fluorescence of cinnamic acid plus BSA in the absence and presence of probe, respectively.…”

Section: )mentioning

confidence: 99%

Studies on the Interaction of Cinnamic Acid with Bovine Serum Albumin

Bian

Zhang

et al. 2007

CHEMICAL & PHARMACEUTICAL BULLETIN

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Cinnamic acid (3-phenyl-2-propenoic acid, structure shown in Fig. 1) is a compound which can be found in nature. It mainly occurs in flavor compositions and products containing cinnamon oil.1) It has a broad possible therapeutic activities, including antimicrobial activity and antifungal activity.2,3) It was shown that cinnamic acid has antitumor activity against human malignant tumors, such as melanoma, glioblastoma and adenocarcinoma of the prostate and lung. 4) It was also approved its use in cancer prevention and therapy because it has low toxicity in rats and rabbits. 1,5) Serum albumin, one of the most available and extensively studied of all proteins, is the most abundant protein in plasma, accounting for about 60% of its total protein content and providing about 80% of the blood osmotic pressure. It plays an important role in drug transport and storage in vertebrates. 6,7) In the current work, bovine serum albumin (BSA) is selected as our protein model because it is well suited to these initial studies and has been extensively characterized.8) BSA consists of 583 amino acids in a single polypeptide chain. It posses a wide range of physiological functions involving the binding, transport and delivery of fatty acids, porphyrins, bilirubin, tryptophan, thyroxin and steroids. It contains three homologous a-helices domains (I, II and III), and each domain is further divided into two subdomains (IA, IB, etc.).9) It posses two tryptophans embedded in two different domains, one of them is located in the proximity of the protein surface, but buried in a hydrophobic pocket of domain I (Trp-134), whereas the other is located in an internal part of domain II (Trp-214).10) Interactions between cinnamic acid and human serum albumin have been reported using Fourier transformed infrared (FT-IR) spectroscopy.11) But BSA has more widely application than human serum albumin because it is not only suitable for humans but also suitable for other animals, and there is lack of information on the cinnamic acid-BSA binding mode, the binding constant, the effects of cinnamic acid complexation on the protein secondary structure, and the effect of common ions. So in this work, the interaction of cinnamic acid and BSA was studied at physiological pH by fluorescence, CD spectroscopy and FT-IR spectroscopy, and the effect of common ions on drug-BSA system in aqueous solutions at physiological pH have also been investigated. Spectroscopic evidence regarding the drug binding mode, the association constant, and the change of protein secondary structure are provided here. ExperimentalMaterials BSA was purchased from Sino-American Biotechnology Company and used without further purification and its molecular weight was 66210. BSA (1.0ϫ10 Ϫ4 mol/l) solution was prepared in pH 7.40 Tris-HCl buffer solution and kept in the dark at 4°C. Cinnamic acid (analytical grade) was obtained from the National Institute for Control Pharmaceutical and Products, China. Cinnamic acid stock solution (1.0ϫ10 Ϫ3 mol/l) was prepared in ethanol. NaCl (analytical ...

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Albumin binding sites for etodolac enantiomers

Cited by 35 publications

References 31 publications

Effect of Ethanol on the Binding of Warfarin Enantiomers to Human Serum Albumin

Effect of Ethanol on the Binding of Warfarin Enantiomers to Human Serum Albumin

Practical Aspects of the Ligand-Binding and Enzymatic Properties of Human Serum Albumin.

Studies on the Interaction of Cinnamic Acid with Bovine Serum Albumin

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