Stereoselective binding and degradation of sulbenicillin in the presence of human serum albumin

Tsuda, Yasuyuki; Tsunoi, Tomoko; Watanabe, Naoko; Ishida, Masato; Yamada, Hideo; Itoh, Tomoo

doi:10.1002/chir.1025

Cited by 8 publications

(6 citation statements)

References 25 publications

(31 reference statements)

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“…Using a similar methodology the authors studied the stereoselective binding and degradation of sulbenicillin, a semisynthetic β-lactam antibiotic, in the presence of HSA (Tsuda et al, 2001). The authors identified at least two types of binding sites on HSA for sulbenicillin enantiomers.…”

Section: Human Serum Albumin Studiesmentioning

confidence: 98%

“…Ultrafiltration combined with chiral separation techniques (Table 1) has been used in the literature for evaluating the stereoselectivity in binding of bimoclomol to HSA, AGP and plasma ; alprenolol to AGP (Imamura et al, 2002) or the tryptophan to bovine serum albumin (BSA) (Randon et al, 2000); warfarin, phenprocoumon and acenocoumarol have been tested for their stereoselective binding to AGP (Hazai et al, 2006); mefloquine to HSA and AGP (Zsila et al, 2008); individual sulbenicillin enantiomers to HSA (Tsuda et al, 2001); ketoprofen to HSA (Lagrange et al, 2000); aminohydantoins in rat, dog and human plasma (Peng et al, 1999); dihydrodiazepam and lorazepam acetate to AGP (Fitos et al, 1995); carbenicillin to HSA (Itoh et al, 1996); antihistamines to HSA; and basic drugs to plasma (Martínez-Gómez et al, 2007a;2007b).…”

Section: Membrane-based Separation Techniquesmentioning

confidence: 99%

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Microseparation techniques for the study of the enantioselectivity of drug–plasma protein binding

Escuder-Gilabert

Martínez-Gómez

Villanueva-Camañas

et al. 2008

Biomedical Chromatography

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Stereoselectivity in protein binding can have a significant effect on the pharmacokinetic and pharmacodynamic properties of chiral drugs. The investigation of enantioselectivity of drugs in their binding with human plasma proteins and the identification of the molecular mechanisms involved in the stereodiscrimination by the proteins represent a great challenge for clinical pharmacology. In this review, the separation techniques used for enantioselective protein binding experiments are described and compared. An overview of studies on enantiomer-protein interactions, enantiomer-enantiomer interactions as well as chiral drug-drug interactions, including allosteric effects, is presented. The contribution of individual plasma proteins to the overall enantioselective binding and the animal species variability in drug-plasma protein binding stereoselectivity are reviewed.

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Section: Human Serum Albumin Studiesmentioning

confidence: 98%

Section: Membrane-based Separation Techniquesmentioning

confidence: 99%

Microseparation techniques for the study of the enantioselectivity of drug–plasma protein binding

Escuder-Gilabert

Martínez-Gómez

Villanueva-Camañas

et al. 2008

Biomedical Chromatography

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“…1,2) Crystallographic studies identified the drug-binding sites I and II, which are two major ligand-binding sites, in subdomains IIA and IIIA, respectively, in the HSA molecule. 2,3) HSA has been reported to exhibit esterase activity to aspirin, 4) sulbenicillin, 5) and diflunisal glucuronide 6) in site I, and p-nitrophenyl acetate, [7][8][9][10] several N-carbobenzoxy-D(L)-alanine p-nitrophenyl esters, 11) and carprofen glucuronide 12) in site II. The esterase-like domain has been assigned to subdomain IIA, at which 199 Lys is important for aspirin hydrolysis, 4) and subdomain IIIA, at which 411 Tyr is important for p-nitrophenyl acetate hydrolysis.…”

mentioning

confidence: 99%

Differences in Esterase Activity to Aspirin and <i>p</i>-Nitrophenyl Acetate among Human Serum Albumin Preparations

Tatsumi

Okada

Inagaki

et al. 2016

Biological & Pharmaceutical Bulletin

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Human serum albumin (HSA) has two major ligand-binding sites, sites I and II, and also hydrolyzes some compounds at both sites. In the present study, we investigated differences in esterase activity among HSA preparations, and also the effects of warfarin, indomethacin, and naproxen on the hydrolytic activities of HSA to aspirin and p-nitrophenyl acetate. The esterase activities of HSA to aspirin or p-nitrophenyl acetate were measured from the pseudo-first-order formation rate constant (k obs ) of salicylic acid or p-nitrophenol by HSA. Inter-lot variations were observed in the esterase activities of HSA to aspirin and p-nitrophenyl acetate; however, the esterase activity of HSA to aspirin did not correlate with that to p-nitrophenyl acetate. The inhibitory effects of warfarin and indomethacin on the esterase activity of HSA to aspirin were stronger than that of naproxen. In contrast, the inhibitory effect of naproxen on the esterase activity of HSA to p-nitrophenyl acetate was stronger than those of warfarin and indomethacin. These results suggest that the administration of different commercial HSA preparations and the co-administration with site I or II high-affinity binding drugs may change the pharmacokinetic profiles of drugs that are hydrolyzed by HSA.

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“…When MK‐0767 was incubated in a protein‐free PBS buffer (pH = 7.0, 7.4, 8.0 and 8.5), the R/S ratio was about 1 (Table 1). The effects of serum albumin have been reported on the epimerization and racemization of a number of drugs 15–19…”

Section: Resultsmentioning

confidence: 99%

Enantiomer ratio of MK‐0767 in humans and nonclinical species

Shen

Bakhtiar

Komuro

et al. 2005

Rapid Comm Mass Spectrometry

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MK-0767, (+/-)-5-[(2,4-dioxothiazolidin-5-yl)methyl]-2-methoxy-N-[[(4-trifluoromethyl)phenyl]methyl]benzamide, is a thiazolidinedione-containing dual peroxisome proliferator-activated receptor (PPAR) alpha/gamma agonist that has been studied as a potential treatment for patients with type 2 diabetes. MK-0767 contains a chiral center at the C-5 position of the thiazolidinedione ring and was being developed as the racemate, due to the rapid interconversion of its enantiomers in biological samples. In the present work the in vitro and in vivo concentration ratios of the (+)-(R) to (-)-(S) enantiomers of MK-0767 were determined in plasma from humans (in vitro only) and nonclinical species used in the toxicological evaluation of rac-MK-0767, namely CD-1 mice, Sprague-Dawley rats, beagle dogs, New Zealand white rabbits, and rhesus monkeys. The R/S ratio was determined by chiral liquid chromatography/tandem mass spectrometry. Species differences were observed in the in vitro and in vivo enantiomeric ratios, as well as differences between in vitro and in vivo in some species. The in vitro R/S ratio was similar in dogs and humans (approximately 1.5-1.7). In rats and monkeys, the ratio was approximately unity, both in vitro and in vivo. In mice, the ratio was higher in vitro (approximately 1) than in vivo (approximately 0.6), while in rabbits it was higher in vivo (approximately 1) than in vitro (approximately 0.5). These results suggested that differential binding of the MK-0767 enantiomers to plasma and tissue proteins and other macromolecules may be affecting the R/S ratio both in vitro and in vivo, since in protein-free systems MK-0767 exists as the racemate.

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Stereoselective binding and degradation of sulbenicillin in the presence of human serum albumin

Cited by 8 publications

References 25 publications

Microseparation techniques for the study of the enantioselectivity of drug–plasma protein binding

Microseparation techniques for the study of the enantioselectivity of drug–plasma protein binding

Differences in Esterase Activity to Aspirin and <i>p</i>-Nitrophenyl Acetate among Human Serum Albumin Preparations

Enantiomer ratio of MK‐0767 in humans and nonclinical species

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