Characterization of site I on human serum albumin: concept about the structure of a drug binding site

Yamasaki, Keishi; Maruyama, Toru; Kragh‐Hansen, Ulrich; Otagiri, Masaki

doi:10.1016/0167-4838(96)00013-1

Cited by 247 publications

(112 citation statements)

References 20 publications

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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

“…To characterize the site in more detail, several attempts to subdivide the site have been made. 8,10,14) In the crystal structures of HSA and rHSA, site I is formed as a pocket in subdomain IIA (Fig. 1A) and involves the lone tryptophan of the protein ( 214 Trp).…”

Section: Ligand Bindingmentioning

confidence: 99%

“…If the latter is the case, the probe-to-protein molar ratios should be kept well below unity to minimize secondary probe binding. Examples of site I probes, in addition to warfarin, are 5-dimethylaminonaphthalene-1-sulfonamide (DNSA), 6) dansylamide, 40,41) dansyl-L-glutamine, 40) dansyl-Lasparagine, 10) dansyl-L-lysine, 42) n-butyl p-aminobenzoate, 10) prodan, 43) and phenol red, 7) and among the site II probes are dansylsarcosine, 6) dansyl-L-proline, 40) dansylglycine, 41) and 7-alkylaminocoumarin-4-acetic acids. 44) Care should be exercised with respect to site I especially, because, as mentioned above, several examples of independent co-binding of two ligands to this site have been reported.…”

Section: Ligand Bindingmentioning

confidence: 99%

“…Endogenous Compounds), and because several examples have been found of independent binding of two different compounds to the site. [7][8][9][10] Several lines of evidence suggest that the site also is very flexible. (i) The fact that ligands with very different chemical structures bind to the region with high affinity indicates that the site is adaptable.…”

Section: Ligand Bindingmentioning

confidence: 99%

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

Kragh‐Hansen

Chuang

Otagiri

2002

Biological & Pharmaceutical Bulletin

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933

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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Section: Ligand Bindingunclassified

Section: Ligand Bindingmentioning

confidence: 99%

Section: Ligand Bindingmentioning

confidence: 99%

Section: Ligand Bindingmentioning

confidence: 99%

See 2 more Smart Citations

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

Kragh‐Hansen

Chuang

Otagiri

2002

Biological & Pharmaceutical Bulletin

Self Cite

933

776

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show abstract

“…Human serum albumin (HSA) contains 585 amino acids, which serves as a transporting agent for various endogenous and exogenous compounds, like fatty acids, nutrients, steroids, certain metal ions, hormones and drugs (Carter et al, 1994;Yamasaki et al, 1996;Pu et al, 2014;Ibrahim et al, 2010). The whole structure is composed of three homologous domains (I, II and III), each could divided into two sub-domains (A and B), and only one tryptophan residue in the sub-domain IIA (Deeb et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Molecular simulation study of the specific combination between four kinds of phthalic acid esters and human serum albumin

Liang

et al. 2016

Environmental Toxicology and Pharmacology

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a b s t r a c tThe interaction between endocrine disruptor phthalic acid esters (PAEs) and human serum albumin (HSA) was studied by fluorescence spectroscopy and molecular modeling methods. The efficiency of energy transfer and the distance between HSA and PAEs were calculated. The results showed that all of the four kinds of PAEs could quench the intrinsic fluorescence of the HSA, with the mechanisms of static quenching and non-radiative energy transfer. Molecular docking study and thermodynamic analysis revealed that the binding behavior was mainly governed by hydrophobic force. And the results of site marker competitive experiments and modeling method suggested that the four PAEs would mainly bind to the HSA in sub-domain IIIA, which demonstrated that the experimental results could coordinate with the theoretical results. Molecular dynamic simulation (MD) revealed that HSA did have a slight conformational change when it bound with PAEs. It also verified the greater stability of HSA-PAEs complex compared to free protein.

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Reversible binding of ethacrynic acid to human serum albumin: Difference circular dichroism study

1999

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The reversible binding of ethacrynic acid was characterized by a difference circular dichroism method. A 2/1 stoichiometry was determined for the [drug]/[HSA] (human serum albumin) complex. The reversible binding of ethacrynic acid to HSA determines direct competition with ligands that selectivity bind to site II and to the fatty acid site. Furthermore, indirect competition was shown for ligands for site I (anticooperative) and to site III (cooperative). Chirality 11:33–38, 1999. © 1999 Wiley‐Liss, Inc.

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Characterization of site I on human serum albumin: concept about the structure of a drug binding site

Cited by 247 publications

References 20 publications

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

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

Molecular simulation study of the specific combination between four kinds of phthalic acid esters and human serum albumin

Reversible binding of ethacrynic acid to human serum albumin: Difference circular dichroism study

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