Displacement of phenprocoumon (Marcumar�) from albumin by sulfonylurea compounds, suramin, and ioglycamic acid

Hüthwohl, B; Jähnchen, E.

doi:10.1007/bf00501412

Cited by 11 publications

(2 citation statements)

References 28 publications

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“…In the present work, the subdomain IB binding of suramin was clearly demonstrated (Figure , Table ). However, effective displacing ability of suramin against the anticoagulant phenprocoumon on BSA has also been reported . Since phenprocoumon is a characteristic site IIA ligand, , this result suggests the contribution of an additional suramin binding site.…”

Section: Case Studiesmentioning

confidence: 94%

“…However, effective displacing ability of suramin against the anticoagulant phenprocoumon on BSA has also been reported. 64 Since phenprocoumon is a characteristic site IIA ligand, 65,66 this result suggests the contribution of an additional suramin binding site. The ICD spectrum of hemin−HSA complexes in which the site IB is completely occupied supports this assumption displaying a large intensity increase upon addition of the drug (Table 7).…”

Section: ■ Case Studiesmentioning

confidence: 98%

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Subdomain IB Is the Third Major Drug Binding Region of Human Serum Albumin: Toward the Three-Sites Model

2013

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According to the conventional view, noncovalent association of small molecules with human serum albumin (HSA) occurs principally at the so-called Sudlow's sites located in subdomain IIA and IIIA. By employing a circular dichroism (CD) spectroscopic approach, it is shown that biliverdin is the specific CD label of an additional drug binding area in subdomain IB. CD competition experiments disclosed the entrapment of a diverse assortment of acidic, neutral, and basic molecules within subdomain IB including anticancer agents (camptothecin, doxorubicin, daunorubicin, teniposide, suramin, tyrosine kinase inhibitors), anticoagulants (dicoumarol), various steroids (bile acids, carbenoxolone), nonsteroidal antiinflammatory drugs, natural substances (aristolochic acid, glycyrrhetinic acid), and synthetic dyes (methyl orange, azocarmine B). These finding imply that subdomain IB can be considered as the third major drug binding region of HSA featured with promiscuous ligand recognition ability. Additionally, subdomain IB is allosterically coupled with the Sudlow's sites, the ligand binding of which is shown to alter the HSA binding mode and affinity of biliverdin and hemin. Brief case studies are presented to illustrate how the evaluation of spectral changes of tetrapyrrole CD probes gains new insight into the HSA binding properties of endogenous as well as pharmaceutical compounds.

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Section: Case Studiesmentioning

confidence: 94%

Section: ■ Case Studiesmentioning

confidence: 98%

Subdomain IB Is the Third Major Drug Binding Region of Human Serum Albumin: Toward the Three-Sites Model

2013

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Vergleichende Untersuchung zur Bindung von Perazindimalonat (PDM) an Human‐ und Rinderserumalbumin

Kinawi

Min

1979

Archiv der Pharmazie

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Der freie Anteil von Perazindimalonat (PDM) in Human-und Rinderserumalbumin-Pufferlosungen @H 7.4) wurde mit Hilfe der durch Ubertragung von HPLC-Techniken optimierten Gelfiltration und Ultrafiltration ermittelt. Die Charakterisierung der Bindung erfolgte durch die Bestirnmung der Gesamtbindungskonstante (Kl), der apparenten Bindungskonstante (k'), der Anzahl der Bindungsstellen/Albuminmolekiil (n) sowie der freien Reaktionsenergie (AFO). Es wurde festge stellt, daf3 der freie Anteil an PDM in den Losungen mit Rinderserumalbumin hoher lag, als in vergleichbaren Losungen mit Humanserumalbumin.Comparative Investigations of the Binding of Perazine Dimalonate (PDM) to Human and Bovine Serum AlbuminThe unbound portion of perazine dimalonate (PDM) in buffered solutionsof human and bovine Serum albumin (pH 7.4) was determined by means of gel filtration and ultrafiltration. Both procedures were optimized by applying techniques which are normaly used in lugh-pressure liquid chromatography. The binding of the drug to serum albumin was characterized by determination of the overall binding constant (K,), the apparent binding constant (k+), the number of binding sites per molecule of albumin (n) and the. free reaction energy (AFO). It was found that less PDM is bound by bovine serum albumin than by human serum albumin.

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The effect of displacement from protein binding on serum and tissue fluid levels of cephazolin

Poláček¹,

Mühlbauer²

1980

Biopharm & Drug Disp

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Displacement of cephazolin, a highly protein-bound beta-lactam antibiotic, by sulpha-phenazole was studied in vitro and in vivo. In vitro, the sulphonamide was effective in displacing the antibiotic from its binding sites at the concentration 100--1000 mumol 1(-1). In vivo, both the serum and the tissue fluid concentration of free cephazolin increased significantly in rats concomitantly treated with sulphaphenazole.

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Displacement of phenprocoumon (Marcumar�) from albumin by sulfonylurea compounds, suramin, and ioglycamic acid

Cited by 11 publications

References 28 publications

Subdomain IB Is the Third Major Drug Binding Region of Human Serum Albumin: Toward the Three-Sites Model

Subdomain IB Is the Third Major Drug Binding Region of Human Serum Albumin: Toward the Three-Sites Model

Vergleichende Untersuchung zur Bindung von Perazindimalonat (PDM) an Human‐ und Rinderserumalbumin

The effect of displacement from protein binding on serum and tissue fluid levels of cephazolin

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