Interactions of Sulfonylureas with Plasma Proteins

Hsu, Par-Lin; Joseph, K. H.; Luzzi, L.A.

doi:10.1002/jps.2600630416

Cited by 26 publications

(7 citation statements)

References 18 publications

(1 reference statement)

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“…However, the order of values was 10 5 in each case (Table 2). Association constant of this order (10 5 ) has also been reported in the literature for some other antidiabetic drugs (4,5). A comparison of the physical properties of the two drugs (Table 1) shows that both the drugs have same total polar surface area and the number of hydrogen bond donors and acceptors.…”

Section: Resultssupporting

confidence: 63%

“…A number of review articles and research papers are available on the interaction of a wide range of drugs with HSA (1–3). Among antidiabetic drugs, some early reports on the interaction of sulphonylureas with plasma proteins are available (4,5). Spectroscopic studies on the molecular basis of the interaction of troglitazone and SU‐118 with HSA have been reported (6,7).…”

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confidence: 99%

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Reversible Binding of Antidiabetic Drugs, Repaglinide and Gliclazide, with Human Serum Albumin

Seedher¹,

Kanojia

2008

Chem Biol Drug Des

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Mechanism of interaction of antidiabetic drugs, repaglinide and gliclazide, to human serum albumin has been studied using fluorescence spectroscopic technique. Repaglinide had much higher affinity for human serum albumin when compared with gliclazide. The order of association constants was 10(5) for both the drugs. The size, hydrophobicity and flexibility of the drug molecules play a major role in explaining the binding behaviour of these drugs. Hydrophobic interactions are predominantly involved in the binding. However, drugs do not share common sites with 1-anilinonaphthalene-8-sulphonate on the human serum albumin molecule. Both tyrosine and tryptophan residues participate in the interaction. Repaglinide and gliclazide are bound to site II on the human serum albumin molecule, and the aromatic ring of 411Tyr appears to be involved in binding within site II. Although they do not bind at site I, their binding at site II may cause conformational changes thereby affecting the binding of other ligands to site I. Site-specificity can be useful in predicting the competitive displacement of these drugs by other co-administered drugs, resulting in fluctuations of the blood glucose levels in diabetic patients. Stern-Volmer analysis of quenching data indicated that the tryptophan residues are not fully accessible to the drugs and predominantly dynamic quenching mechanism is involved in the binding.

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Section: Resultssupporting

confidence: 63%

mentioning

confidence: 99%

Reversible Binding of Antidiabetic Drugs, Repaglinide and Gliclazide, with Human Serum Albumin

Seedher¹,

Kanojia

2008

Chem Biol Drug Des

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“…Thus, it seems that the binding characteristics ofthese two 'N-d-N compounds' are different from that of other sulphonylureas (Hsu et al, 1974). It is not possible, however, to extrapolate these results to the increased potency of glipizide and glibenclamide, even if it has been shown that, in contrast to tolbutamide, glibenclamide penetrates pancreatic cells well despite its higher molecular size (Hellman et al, 1973).…”

Section: Protein Bindingmentioning

confidence: 93%

Clinical Pharmacokinetics of Sulphonylurea Hypoglycaemic Drugs

Balant

1981

Clinical Pharmacokinetics

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“…The mechanism of interaction of a wide range of drugs with human serum albumin has been reported in the literature [1][2][3]. Amongst antidiabetic drugs, such studies on some sulfonylureas and troglitazone are available [4][5].…”

Section: Introductionmentioning

confidence: 99%

Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin

Seedher

Kanojia

2009

Open Chemistry

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Abstract:The mechanism of interaction of hypoglycemic drugs, glimepiride and glipizide with human serum albumin (HSA) has been studied using fluorescence spectroscopy. The results are discussed in terms of the binding parameters, thermodynamics of the binding process, nature of forces involved in the interaction, identification of drug binding site on serum albumin and the fluorescence quenching mechanism involved. The association constants were of the order of 10 5 and glipizide was found to have much higher affinity for HSA than glimepiride at all temperatures. Thermodynamic parameters for the binding suggested that hydrophobic interactions are primarily involved in the binding of these drugs to HSA. However, glimepiride and glipizide appear to cause temperature-dependent conformational changes in the albumin molecule and, therefore, the nature of interaction varied with temperature. Glimepiride and glipizide bind to both site I and site II on HSA, but the primary interaction occurs at site II. The binding region in site II is different for the two drugs. Stern-Volmer analysis of quenching data indicated that tryptophan residues of HSA are not fully accessible to the drugs and a predominantly dynamic quenching mechanism is involved in the binding. Results can provide useful insight into prediction of competitive displacement of these drugs by other co-administered drugs and excipients, resulting in serious fluctuations of the blood glucose levels in diabetic patients.

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Interactions of Sulfonylureas with Plasma Proteins

Cited by 26 publications

References 18 publications

Reversible Binding of Antidiabetic Drugs, Repaglinide and Gliclazide, with Human Serum Albumin

Reversible Binding of Antidiabetic Drugs, Repaglinide and Gliclazide, with Human Serum Albumin

Clinical Pharmacokinetics of Sulphonylurea Hypoglycaemic Drugs

Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin

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