Stability of warfarin solutions for drug–protein binding measurements: Spectroscopic and chromatographic studies

Moser, Annette C.; Kingsbury, Charles A.; Hage, David S.

doi:10.1016/j.jpba.2006.02.012

Cited by 28 publications

(42 citation statements)

References 34 publications

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“…The solutions of R- warfarin were prepared in this mobile phase and filtered through a 0.2 μm nylon filter, followed by a 15 min degassing step prior to use. All solutions and samples containing R- warfarin were used within two weeks of preparation to ensure stable conditions for drug-protein binding measurements [21,22,38]. The L-tryptophan solutions were prepared fresh daily in the same pH 7.4 buffer, as described previously [21,22,39].…”

Section: Methodsmentioning

confidence: 99%

Chromatographic analysis of the effects of fatty acids and glycation on binding by probes for Sudlow sites I and II to human serum albumin

Anguizola

DeBolt

Suresh

et al. 2016

Journal of Chromatography B

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The primary endogenous ligands of human serum albumin (HSA) are non-esterified fatty acids, with 0.1–2 moles of fatty acids normally being bound to HSA. In type II diabetes, fatty acid levels in serum are often elevated, and the presence of high glucose results in an increase in the non-enzymatic glycation of HSA. High-performance affinity chromatography (HPAC) was used to examine the combined effects of glycation and the presence of long chain fatty acids on the binding of HSA with R-warfarin and L-tryptophan (i.e., probes for Sudlow sites I and II, the major sites for drugs on this protein). Zonal elution competition studies were used to examine the interactions of myristic acid, palmitic acid and stearic acid with these probes on HSA. It was found that all these fatty acids had direct competition with R-warfarin at Sudlow site I of normal HSA and glycated HSA, with the glycated HSA typically having stronger binding for the fatty acids at this site. At Sudlow site II, direct competition was observed for all the fatty acids with L-tryptophan when using normal HSA, while glycated HSA gave no competition or positive allosteric interactions between these fatty acids and L-tryptophan. These data indicated that glycation can alter the interactions of drugs and fatty acids at specific binding sites on HSA. The results of this study should lead to a better understanding of how these interactions may change during diabetes and demonstrate how HPAC can be used to examine drug/solute-protein interactions in complex systems.

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Section: Methodsmentioning

confidence: 99%

Chromatographic analysis of the effects of fatty acids and glycation on binding by probes for Sudlow sites I and II to human serum albumin

Anguizola

DeBolt

Suresh

et al. 2016

Journal of Chromatography B

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“…Warfarin is an anticoagulant drug known to bind to Sudlow site I [31,34], while carbamazepine is an anticonvulsant drug that binds to Sudlow site II [35–37]. The binding of both of these drugs has previously been examined using traditional HPLC affinity columns in which HSA has been immobilized to silica particles [34,36,38–40]. …”

Section: Introductionmentioning

confidence: 99%

Evaluation of silica monoliths in affinity microcolumns for high‐throughput analysis of drug–protein interactions

Yoo

Hage²

2009

J of Separation Science

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Silica monoliths in affinity microcolumns were tested for the high-throughput analysis of drugprotein interactions. Human serum albumin (HSA) was used as a model protein for this work, while carbamazepine and R-warfarin were used as model analytes. A comparison of HSA silica monoliths of various lengths indicated columns as short as 1 to 3 mm could be used to provide reproducible estimates of retention factors or plate heights. Benefits of using smaller columns for this work included the lower retention times and lower back pressures that could be obtained versus traditional HPLC affinity columns, as well as the smaller amount of protein that is required for column preparation. One disadvantage of decreasing column length was the lower precision that resulted in retention factor and plate height measurements. A comparison was also made between microcolumns containing silica particles versus silica monoliths. It was demonstrated with R-warfarin that supports could be used in HSA microcolumns for the determination of retention factors or plate heights. However, the higher efficiency of the silica monolith made this the preferred support for work at higher flow rates or when a larger number of plates are needed during the rapid analysis of drug-protein interactions.

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“…15) It has been reported that the conversion of the cyclic hemiketal form of warfarin affects the binding of S-and R-warfarin to HSA. 16) Ethanol may also affect on the conversion of the cyclic hemiketal form of warfarin.…”

Section: Discussionmentioning

confidence: 99%

Effect of Ethanol on the Binding of Warfarin Enantiomers to Human Serum Albumin

Tatsumi

Kadobayashi

Iwakawa

2007

Biological & Pharmaceutical Bulletin

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Ethanol is widely used as a pharmaceutical excipient for the solubilization of many hydrophobic drugs for injections. However, there are only few studies about drug interaction with pharmaceutical excipients in the body after injection. In this study, the effect of ethanol (500 mM) or several alcohols (500 mM) on the stereoselective binding of warfarin enantiomers to fatty acid-free human serum albumin (HSA) or proteins of commercial albumin preparations was investigated. An ultrafiltration method was used for the separation of unbound warfarin enantiomers. By the addition of ethanol or 1-propanol, the unbound fraction of the S-enantiomer was decreased. On the other hand, the unbound fraction of the R-enantiomer was increased by the addition of ethanol or 1-propanol. Unbound fractions of both the S-and R-enantiomer were decreased by 2-propanol. In various commercial albumin preparations, unbound fractions of both the S-and R-enantiomer were increased by ethanol. The different effects of ethanol among fatty acid-free HSA and commercial albumin preparations were observed.

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Stability of warfarin solutions for drug–protein binding measurements: Spectroscopic and chromatographic studies

Cited by 28 publications

References 34 publications

Chromatographic analysis of the effects of fatty acids and glycation on binding by probes for Sudlow sites I and II to human serum albumin

Chromatographic analysis of the effects of fatty acids and glycation on binding by probes for Sudlow sites I and II to human serum albumin

Evaluation of silica monoliths in affinity microcolumns for high‐throughput analysis of drug–protein interactions

Effect of Ethanol on the Binding of Warfarin Enantiomers to Human Serum Albumin

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