Comparison of drug binding interactions on human, rat and rabbit serum albumin using high-performance displacement chromatography

Aubry, Anne‐Françoise; Markoglou, Nektaria; McGann, Angela

doi:10.1016/0742-8413(95)02019-5

Cited by 22 publications

(18 citation statements)

References 7 publications

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“…This is often done with zonal elution and competition studies through the use of an injected probe that has a known binding site on a protein such as HSA. This type of experiment, which was illustrated earlier in Figure 2 and Figure 3(a), has been used to investigate the binding of HSA and other albumins with non-steroidal anti-inflammatory drugs [132,133], R - and S -ibuprofen [134], cis - and trans -clomiphene [135], digitoxin or acetyldigitoxin [136], benzodiazepines [137], phenytoin [138], carbamazepine [122], L-thyroxine [116] and verapamil [60]. Probe compounds that have been employed in such work include R / S -warfarin, L-tryptophan, phenylbutazone, R / S -ibuprofen, 2,3,5-triiodobenzoic acid, cis / trans -clomiphene, acetyldigitoxin, digitoxin, and phenol red [60,116,122,132–138].…”

Section: Hpac Studies Of Hsa and Other Serum Albuminsmentioning

confidence: 99%

Characterization of drug–protein interactions in blood using high‐performance affinity chromatography

Hage

Jackson

Sobansky

et al. 2009

J of Separation Science

144

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The binding of drugs with proteins in blood, serum or plasma is an important process in determining the activity, distribution, rate of excretion, and toxicity of drugs in the body. Highperformance affinity chromatography (HPAC) has received a great deal of interest as a means for studying these interactions. This review examines the various techniques that have been used in HPAC to examine drug-protein binding and discusses the types of information that can be obtained through this approach. A comparison of these techniques with traditional methods for binding studies (e.g., equilibrium dialysis and ultrafiltration) will also be presented. The use of HPAC with specific serum proteins and binding agents will then be discussed, including human serum albumin and α 1 -acid glycoprotein. Several examples from the literature are provided to illustrate the applications of such research. Recent developments in this field are also described, such as the use of improved immobilization techniques, new data analysis methods, techniques for working for directly with complex biological samples, and work with immobilized lipoproteins. The relative advantages and limitations of the methods that are described will be considered and the possible use of these techniques in the high-throughput screening or characterization of drugprotein binding will be discussed.

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Section: Hpac Studies Of Hsa and Other Serum Albuminsmentioning

confidence: 99%

Characterization of drug–protein interactions in blood using high‐performance affinity chromatography

Hage

Jackson

Sobansky

et al. 2009

J of Separation Science

144

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“…Second, comparative studies between rodent and human albumin indicate that there are structural differences in the binding sites of the two albumins as well as quantitative differences with respect to the extent of drug binding (6,65). In general, protein binding for most antimicrobials is lower in rodents than it is in humans (29).…”

Section: Problems and Challenges Of Current Modelsmentioning

confidence: 99%

Protein Binding: Do We Ever Learn?

Zeitlinger

Derendorf

Mouton

et al. 2011

Antimicrob Agents Chemother

218

194

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6Although the influence of protein binding (PB) on antibacterial activity has been reported for many antibiotics and over many years, there is currently no standardization for pharmacodynamic models that account for the impact of protein binding of antimicrobial agents in vitro. This might explain the somewhat contradictory results obtained from different studies. Simple in vitro models which compare the MIC obtained in protein-free standard medium versus a protein-rich medium are prone to methodological pitfalls and may lead to flawed conclusions. Within in vitro test systems, a range of test conditions, including source of protein, concentration of the tested antibiotic, temperature, pH, electrolytes, and supplements may influence the impact of protein binding. As new antibiotics with a high degree of protein binding are in clinical development, attention and action directed toward the optimization and standardization of testing the impact of protein binding on the activity of antibiotics in vitro become even more urgent. In addition, the quantitative relationship between the effects of protein binding in vitro and in vivo needs to be established, since the physiological conditions differ. General recommendations for testing the impact of protein binding in vitro are suggested.Binding to plasma proteins plays a major role in drug therapy as this binding provides a depot for many compounds, affects pharmacokinetics (PK) and pharmacodynamics (PD) of drugs, and may influence the metabolic modification of ligands (34,104). Protein binding (PB) of antibiotics may affect the efficacy of antimicrobial therapy in two ways. First, only the non-protein-bound fraction of a drug in plasma can penetrate into and equilibrate with the extravascular space (13). Penetration into the extravascular space is highly important for antimicrobial therapy, as the majority of bacterial and fungal infections occur in the interstitial fluid of tissues or in other body fluids than blood (113). PB also affects drug clearance from the body. For antibiotics eliminated by tubular secretion or hepatic metabolism, high PB is associated with lowered drug elimination. Additionally, PB negatively correlates with glomerular filtration, since only the free drug is filtered (63). On the other hand, small fluctuations in protein binding usually have no effect on average unbound concentrations, and this is especially the case for drugs with a low extraction ratio (11). Changes in protein binding can also alter the volume of distribution and, hence, the half-life, which may, in turn, modify the time above MIC. Extensive reviews on the impact of PB on pharmacokinetics of drugs are available (12,13,27,29,82,86).The second effect of PB is demonstrated by the impact on the antibacterial activity. Over many decades, various methods were used to show that only the non-protein-bound fraction of an antibiotic is microbiologically active (10,28,70,111). For important antibiotic classes, such as penicillins and quinolones, clear relationships between the percenta...

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“…non-specific analyte-amino acid and solute-silica interactions). Thus, displacement chromatography data can be used to study pharmacologically relevant saturable interactions, and to distinguish between direct and indirect competition when co-binding of two drugs to the protein occurs [6,72,[82][83][84][97][98][99][100][101][102][103][104][105][106]. Most of these studies have been carried out using as competitors drugs that bind to Sites I and II, like profens, benzodiazepines, phenylbutazone, warfarin, salicylate, and valproate.…”

Section: Determination Of Drug-drug Protein Binding Interactionsmentioning

confidence: 98%

Drug affinity to immobilized target bio-polymers by high-performance liquid chromatography and capillary electrophoresis

Bertucci¹,

Bartolini²,

Gotti³

et al. 2003

Journal of Chromatography B

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Comparison of drug binding interactions on human, rat and rabbit serum albumin using high-performance displacement chromatography

Cited by 22 publications

References 7 publications

Characterization of drug–protein interactions in blood using high‐performance affinity chromatography

Characterization of drug–protein interactions in blood using high‐performance affinity chromatography

Protein Binding: Do We Ever Learn?

Drug affinity to immobilized target bio-polymers by high-performance liquid chromatography and capillary electrophoresis

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