Characterizing a Drug’s Primary Binding Site on Albumin

Day, Yasmina S.N.; Myszka, David G.

doi:10.1002/jps.10293

Cited by 86 publications

(56 citation statements)

References 13 publications

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“…In the blood, various plasma proteins are able to bind with certain drug, increase the molecule weight, make it difficult to across the cell membrane and loss activity temporarily (Buxton 2006). Thereby, plasma protein provides a reservoir that regulates the equilibrium of bound and unbound form of the drug in circulation (Day and Myszka 2002). For a certain drug, variation of plasma protein composition could obviously influence its binding capacity.…”

Section: Discussionmentioning

confidence: 99%

Why mammals more susceptible to the hepatotoxic microcystins than fish: evidences from plasma and albumin protein binding through equilibrium dialysis

Zhang

Gao

et al. 2013

Ecotoxicology

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To elucidate the interspecies variation of susceptibility to microcystins (MCs), fresh plasma and purified albumin from six kinds of mammals and fish were used in toxins-substances binding test. Protein contents in the test plasma were analyzed and the binding characteristics to MCs were compared. Two kinds of widely observed MCs, microcystin-LR (MC-LR) and microcystin-RR (MC-RR) were tested and data were collected through the method of equilibrium dialysis. It was found that total plasma protein and albumin content in mammals were nearly two times and four times higher than that in fish, respectively. In the test range of 0-100 lg/mL, binding rates of fish plasma to MCs were considered significant lower (p \ 0.01) than that of mammals. And human plasma demonstrated the highest binding rate in mammals. In all the test species, plasma protein binding rates of MC-RR were significantly higher than MC-LR (p \ 0.01). Besides, binding profiles of albumin were acquired under the protein content of 0.67 mg/mL. Human serum albumin demonstrated the highest affinity to MCs throughout the six species and differences among the other five species were considered not significant (p [ 0.05). From the view of protein binding, it is concluded that both the variation of plasma protein composition and albumin binding characteristic could influence the existing form of MCs in circulation, change MCs utilization, alter MCs half-life and further contribute to the difference of susceptibility between mammals and fish.

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Section: Discussionmentioning

confidence: 99%

Why mammals more susceptible to the hepatotoxic microcystins than fish: evidences from plasma and albumin protein binding through equilibrium dialysis

Zhang

Gao

et al. 2013

Ecotoxicology

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“…The affinity of the binding of compounds to bovine BSA, bovine FAF BSA, and sheep g-globulin was assessed by surface plasmon resonance analysis on a BiaCore S51 instrument as described previously for binding studies using human serum albu-min (68)(69)(70)…”

Section: Flow Cytometric Analysis Of Sr-bi Cell Surface Expressionmentioning

confidence: 99%

Influence of HDL-cholesterol-elevating drugs on the in vitro activity of the HDL receptor SR-BI

Nieland

Shaw

Jaipuri

et al. 2007

Journal of Lipid Research

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Treatment of atherosclerotic disease often focuses on reducing plasma LDL-cholesterol or increasing plasma HDL-cholesterol. We examined in vitro the effects on HDL receptor [scavenger receptor class B type I (SR-BI)] activity of three classes of clinical and experimental plasma HDL-cholesterol-elevating compounds: niacin, fibrates, and HDL376. Fenofibrate (FF) and HDL376 were potent (IC 50 ? 1 mM), direct inhibitors of SR-BI-mediated lipid transport in cells and in liposomes reconstituted with purified SR-BI. FF, a prodrug, was a more potent inhibitor of SR-BI than an activator of peroxisome proliferator-activated receptor a, a target of its active fenofibric acid (FFA) derivative. Nevertheless, FFA, four other fibrates (clofibrate, gemfibrozil, ciprofibrate, and bezafibrate), and niacin had little, if any, effect on SR-BI, suggesting that they do not directly target SR-BI in vivo. However, similarities of HDL376 treatment and SR-BI gene knockout on HDL metabolism in vivo (increased HDL-cholesterol and HDL particle sizes) and structure-activity relationship analysis suggest that SR-BI may be a target of HDL376 in vivo. HDL376 and other inhibitors may help elucidate SR-BI function in diverse mammalian models and determine the therapeutic potential of SR-BI-directed pharmaceuticals.-Nieland, T.

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“…From the surface plasmon resonance (SPR) curve shown in Figure 2.26, not only can the binding strength be calculated, but also the onset and offset rates of the binding. Day and Myszka [96] described a procedure in detail for the characterization of compounds binding to the albumin major binding sites. Oravcova et al [54] have reviewed the application of chromatographic principles in affinity chromatography and size exclusion chromatography.…”

Section: Methods Based On the Principle Of Frontal Chromatographymentioning

confidence: 99%

Application of High Performance Liquid Chromatography for the Measurements of Lipophilicity and Biomimetic Binding Properties in Drug Discovery

Valkó¹

2012

Physico-Chemical Methods in Drug Discovery and Development

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Characterizing a Drug’s Primary Binding Site on Albumin

Cited by 86 publications

References 13 publications

Why mammals more susceptible to the hepatotoxic microcystins than fish: evidences from plasma and albumin protein binding through equilibrium dialysis

Why mammals more susceptible to the hepatotoxic microcystins than fish: evidences from plasma and albumin protein binding through equilibrium dialysis

Influence of HDL-cholesterol-elevating drugs on the in vitro activity of the HDL receptor SR-BI

Application of High Performance Liquid Chromatography for the Measurements of Lipophilicity and Biomimetic Binding Properties in Drug Discovery

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