Some novel observations of a drug (indoprofen)—albumin interaction

Juni, Kazuhiko; Nieves, Estela; Perrin, John H.

doi:10.1002/bdd.2510040103

Cited by 6 publications

(1 citation statement)

References 5 publications

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“…On the other hand, in the endothermic effects of [C(4) mim] + , [C(6)mim] + , [C(8)mim] + and [C(10)mim] + , binding to HSA is observed (Table 5). According to the literature, this may be attributed to low degrees of saturation of HSA being related to relatively low concentrations (Juni et al 1983) and indicates that imidazolium cations bind to HSA via ionic and hydrophobic interactions (Ross et al 1981). Nevertheless, the delocalization of the positive charge onto the large imidazolium ring may induce weaker electrostatic interactions between HSA and imidazolium cations (Liu et al 2013).…”

Section: Determination Of the Enthalpy Value (δH) Of Hsa-il Interactionsmentioning

confidence: 99%

Interaction of ionic liquids with human serum albumin in the view of bioconcentration: a preliminary study

et al. 2022

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Bioaccumulation potential is critical in PBT and risk assessment of chemicals. However, for ionic liquids (ILs), this aspect remains neglected. It is especially important to fill this gap, because for this group of compounds, existing data confirm their risk of being environmentally persistent and toxicity. Moreover, considering preliminary reports on the interactions of ILs with lipids, it may be assumed that ILs have a higher potential for bioaccumulation than indicated by previous estimations built upon octanol–water partition coefficients. Moreover, the bioconcentration of ionizable chemical compounds may also be strongly related to plasma protein contents. Therefore, in this work, the affinity of a set of imidazolium cations and organic anions, and their combination to human serum albumin (HSA) was determined. The obtained results reveal that both cations and anions can be strongly bound to HSA, and blood proteins might play an important role in overall bioaccumulation. Furthermore, it was observed that HSA binding properties towards IL cations depend on the hydrophobicity of cations. The obtained data also provide indication that cation–anion interaction may affect ILs ions affinity to HSA.

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Section: Determination Of the Enthalpy Value (δH) Of Hsa-il Interactionsmentioning

confidence: 99%

Interaction of ionic liquids with human serum albumin in the view of bioconcentration: a preliminary study

et al. 2022

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The effect of Ca⁺⁺ on the binding of drugs to human serum albumin: Pharmacokinetic implications

Perrin

Juni

1982

Biopharm & Drug Disp

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A Recenthave shown dramatic effects of C a + + on the binding of drugs to human serum albumin (HSA). For example, dialysis studies showed that the binding of warfarin was increased over the pH range 5-9 following the addition of C a + + . This was apparently due to the effect of the ion on the N-B (neutral-basic) equilibrium of the HSA, the equilibrium occurring over this same pH range. On the other hand CI-at physiological concentrations was found to reduce the binding of warfarin to HSA by a competitive binding mechanism. Subsequently M g + + was found to reduce the binding of warfarin to HSA when the protein was in the B form, but there was little effect at the physiological P H .~ On the other hand Ca+ + was found to reduce the binding of diazepam3 and benoxaprofen4 to HSA, over the pH range of the N-B conformational change. These drugs do not share a primary binding site with warfarin.'. ' This phenomenon may be due to competition between Ca' + and the drugs for the imidazole residues at the binding sites.4 The interesting possibility arises of Ca+ + being used as a marker to determine which of the two major and independent binding sites (the warfarin or the diazepam site') on HSA, a given drug has as its primary binding site. The work reported in Table 1 was primarily designed to test this possibility.Dialysis was conducted as previously described2a4 using 0.1 M sodium chloride with the pH adjusted with sodium hydroxide or hydrochloric acid, with and without 2.5 x M calcium chloride at 25". N o clear cut pattern arises as far as the assignment of binding sites from the effect of the C a + + on the extent of binding. This is assuming that the assignment of binding sites in the literature is correct.'. ' The data in the table, especially for salicyclic acid, phenytoin, dicumarol, ibuprofen, diazepam, and benoxaprofen, stress the dramatic effect C a + + can have on the extent of binding of drugs to HSA and, although 0

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Microcalorimetric investigations of drug–albumin interactions

Hardee

Fleitman

Otagiri

et al. 1984

Biopharm & Drug Disp

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Flow microcalorimetry was used to estimate primary binding constants for drug-albumin interactions. Measurements of heat of reaction at two temperatures illustrated the danger of extrapolation for pharmacokinetic purposes of measurements made at temperatures other than 37 degrees. The method could be used to predict competition between two drugs for a single binding site. Major advantages over spectroscopic techniques included direct determinations of thermodynamic parameters, and the use of physiological concentrations of albumin.

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Some novel observations of a drug (indoprofen)—albumin interaction

Cited by 6 publications

References 5 publications

Interaction of ionic liquids with human serum albumin in the view of bioconcentration: a preliminary study

Interaction of ionic liquids with human serum albumin in the view of bioconcentration: a preliminary study

The effect of Ca⁺⁺ on the binding of drugs to human serum albumin: Pharmacokinetic implications

Microcalorimetric investigations of drug–albumin interactions

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Some novel observations of a drug (indoprofen)—albumin interaction

Cited by 6 publications

References 5 publications

Interaction of ionic liquids with human serum albumin in the view of bioconcentration: a preliminary study

Interaction of ionic liquids with human serum albumin in the view of bioconcentration: a preliminary study

The effect of Ca++ on the binding of drugs to human serum albumin: Pharmacokinetic implications

Microcalorimetric investigations of drug–albumin interactions

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The effect of Ca⁺⁺ on the binding of drugs to human serum albumin: Pharmacokinetic implications