Stereoselective binding of the glucuronide of ketoprofen enantiomers to human serum albumin

Dubois, Nathalie; Lapicque, Françoise; Magdalou, Jacques; Abiteboul, M; Netter, Patrick

doi:10.1016/0006-2952(94)90453-7

Cited by 19 publications

(12 citation statements)

References 24 publications

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“…The stereospecific degradation and in vitro covalent protein binding of b-1-O-acyl glucuronide metabolites of chiral NSAIDs have been studied for R/S-carprofen, 31,32 R/S-fenoprofen, 33,34 R/S-ketoprofen, 10,35,36 and R/S-naproxen. 21 Also, the stereospecific degradation of b-1-O-acyl glucuronides of the model compound R/S-2-phenylpropionic acid has been studied.…”

Section: à8mentioning

confidence: 99%

Stereospecific pH‐dependent degradation kinetics of R‐ and S‐naproxen‐β‐l‐O‐acyl‐glucuronide

et al. 2002

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The hydrolysis and acyl migration of biosynthetic S-naproxen-beta-l-O-acyl glucuronide (I) and R-naproxen-beta-l-O-acyl glucuronide (II) was followed by HPLC. Nine first-order kinetic rate constants for the hydrolysis and acyl migration between the beta-l-O-acyl glucuronide, its alpha/beta-2, alpha/beta-3-, alpha/beta-4-, and alpha-1-O-acyl isomers and naproxen aglycone were determined for I and II at pH 7.00, 7.40 and 8.00 at 37 degrees C by kinetic simulation. For I the 3-O-acyl isomer was the most stable isomer as the pseudo-equilibrium ratio for the major acyl-migrated isomers was 1:1.5:0.9 (2-O-acyl isomer:3-O-acyl isomer:4-O-acyl isomer). The 3- and 4-O-acyl isomers of II were equally stable as the pseudo-equilibrium ratio for the major acyl-migrated isomers was 1:1.4:1.4 (2-O-acyl isomer:3-O-acyl isomer:4-O-acyl isomer). For both I and II, the pseudo-equilibrium ratio between the major 2-O-acyl isomer and the minor alpha-l-O-acyl isomer was 10:1 (2-O-acyl isomer:alpha-l-O-acyl isomer). The pseudo-equilibrium found for the major acyl-migrated isomers of I and II in the present study corresponds with the pattern previously published for R- and S-ketoprofen-beta-l-O-acyl glucuronide acyl-migrated isomers, suggesting that these findings may be general for acyl-migrated beta-l-O-acyl glucuronides of enantiomeric 2-arylpropionic acids.

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Section: à8mentioning

confidence: 99%

Stereospecific pH‐dependent degradation kinetics of R‐ and S‐naproxen‐β‐l‐O‐acyl‐glucuronide

et al. 2002

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“…Energy transfer from BSA to LP: Fluorescence resonance energy transfer is an important technique for investigating a variety of biological phenomena including energy transfer processes 26 . Here the donor and acceptor are BSA and LP, respectively.…”

Section: Binding Sites Of Lp On the Bsamentioning

confidence: 99%

Untitled

2016

IJPSR

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ABSTRACT:The interaction of losartan potassium (LP) with bovine serum albumin (BSA) was studied by fluorescence quenching in combination with UV-Vis spectroscopic method under near physiological conditions. The fluorescence quenching rate constants and binding constants for BSA-LP system were determined at different temperatures. The fluorescence quenching of BSA by LP is due to static quenching and energy transfer. The results of thermodynamic parameters, ∆H (-134.3 kJ mol ) and ∆G (-24.52 to -20.83 kJ mol -1 ), indicated that van der Waals interaction and hydrogen bonding played a major role for LP-BSA association. The competitive experiments demonstrated that the primary binding site of LP on BSA was located at site II in sub-domain IIIA of BSA. The distance between LP and a tryptophane unit was estimated to be 3.183 nm based on the Förster resonance energy transfer theory. The binding constant (Ka) of BSA-LP at 298K was 1.932×104 L mol -1 . Synchronous fluorescence and three-dimensional fluorescence studies showed that the presence of LP could change the conformation of BSA during the binding process.

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“…When KP binds to HSA, a specific Cotton effect will be induced (Dubois et al, 1994;Zandomeneghi, 1995). Figure 2 shows the CD spectra obtained when KP was added to the different albumin solutions.…”

Section: Binding Parameters Of Kp To Albumins Of Different Speciesmentioning

confidence: 99%

Subdomain IIIA of Dog Albumin Contains a Binding Site Similar to Site II of Human Albumin

Kaneko

Fukuda²,

Chuang

et al. 2007

Drug Metab Dispos

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Stereoselective binding of the glucuronide of ketoprofen enantiomers to human serum albumin

Cited by 19 publications

References 24 publications

Stereospecific pH‐dependent degradation kinetics of R‐ and S‐naproxen‐β‐l‐O‐acyl‐glucuronide

Stereospecific pH‐dependent degradation kinetics of R‐ and S‐naproxen‐β‐l‐O‐acyl‐glucuronide

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Subdomain IIIA of Dog Albumin Contains a Binding Site Similar to Site II of Human Albumin

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