Analysis of stereoselective drug interactions with serum proteins by high-performance affinity chromatography: A historical perspective

Zhao, Liang; Hage, David S.

doi:10.1016/j.jpba.2017.01.026

Cited by 28 publications

(20 citation statements)

References 147 publications

(287 reference statements)

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“…Plasma proteins are capable of interacting with about 43% of the 1500 drugs most commonly used in clinical practice [1,2]. Moreover, the drugs frequently show a high affinity for these proteins (about 90% or more of the administered dose binds to plasma proteins) [3].…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, the drugs frequently show a high affinity for these proteins (about 90% or more of the administered dose binds to plasma proteins) [3]. Consequently, the interaction between drugs and plasma proteins is quite significant, which is reflected in the biological action of drugs [1,2]. It should be noted that the interactions established between proteins and drugs are reversible, since the purpose is to transport the compounds to the different tissues in order to achieve their biotargets.…”

Section: Introductionmentioning

confidence: 99%

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Enantioresolution and Binding Affinity Studies on Human Serum Albumin: Recent Applications and Trends

et al. 2021

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The interaction between proteins and drugs or other bioactive compounds has been widely explored over the past years. Several methods for analysis of this phenomenon have been developed and improved. Nowadays, increasing attention is paid to innovative methods, such as high performance affinity liquid chromatography (HPALC) and affinity capillary electrophoresis (ACE), taking into account various advantages. Moreover, the development of separation methods for the analysis and resolution of chiral drugs has been an area of ongoing interest in analytical and medicinal chemistry research. In addition to bioaffinity binding studies, both HPALC and ACE al-low one to perform other type of analyses, namely, displacement studies and enantioseparation of racemic or enantiomeric mixtures. Actually, proteins used as chiral selectors in chromatographic and electrophoretic methods have unique enantioselective properties demonstrating suitability for the enantioseparation of a large variety of chiral drugs or other bioactive compounds. This review is mainly focused in chromatographic and electrophoretic methods using human serum albumin (HSA), the most abundant plasma protein, as chiral selector for binding affinity analysis and enantioresolution of drugs. For both analytical purposes, updated examples are presented to highlight recent applications and current trends.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Enantioresolution and Binding Affinity Studies on Human Serum Albumin: Recent Applications and Trends

et al. 2021

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“…Various analytical techniques that have been used to characterize biomolecular interactions. Some of these techniques include affinity-based separation techniques, which represent the major domain of affinity chromatography, [4][5][6] and affinity capillary electrophoresis [7][8][9] as well as equilibrium dialysis, which is still interesting and widely used especially in drug-protein interaction studies [10][11][12]. On the other hand, biochemical and biophysical techniques are attractive and developed dramatically to be the first choice in studying biomolecular interactions.…”

Section: Introductionmentioning

confidence: 99%

Thermophoresis for characterizing biomolecular interaction

Asmari

Ratih

Alhazmi

et al. 2018

Methods

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The study of biomolecular interactions is crucial to get more insight into the biological system. The interactions of protein-protein, protein-nucleic acids, protein-sugars, nucleic acid-nucleic acids and protein-small molecules are supporting therapeutics and technological developments. Recently, the development in a large number of analytical techniques for characterizing biomolecular interactions reflect the promising research investments in this field. In this review, microscale thermophoresis technology (MST) is presented as an analytical technique for characterizing biomolecular interactions. Recent years have seen much progress and several applications established. MST is a powerful technique in quantitation of binding events based on the movement of molecules in microscopic temperature gradient. Simplicity, free solutions analysis, low sample volume, short analysis time, and immobilization free are the MST advantages over other competitive techniques. A wide range of studies in biomolecular interactions have been successfully carried out using MST, which tend to the versatility of the technique to use in screening binding events in order to save time, cost and obtained high data quality.

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“…Nevertheless, the number of publications describing the use of protein-based CSPs has been decreasing over the years [ 117 , 136 ]. Binding affinity studies between drugs and proteins and drug-protein interactions were also found [ 137 , 138 , 139 ].…”

Section: Chiral Stationary Phases: Recent Developmentsmentioning

confidence: 99%

Chiral Stationary Phases for Liquid Chromatography: Recent Developments

et al. 2019

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The planning and development of new chiral stationary phases (CSPs) for liquid chromatography (LC) are considered as continuous and evolutionary issues since the introduction of the first CSP in 1938. The main objectives of the development strategies were to attempt the improvement of the chromatographic enantioresolution performance of the CSPs as well as enlarge their versatility and range of applications. Additionally, the transition to ultra-high-performance LC were underscored. The most recent strategies have comprised the introduction of new chiral selectors, the use of new materials as chromatographic supports or the reduction of its particle size, and the application of different synthetic approaches for preparation of CSPs. This review gathered the most recent developments associated to the different types of CSPs providing an overview of the relevant advances that are arising on LC.

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Analysis of stereoselective drug interactions with serum proteins by high-performance affinity chromatography: A historical perspective

Cited by 28 publications

References 147 publications

Enantioresolution and Binding Affinity Studies on Human Serum Albumin: Recent Applications and Trends

Enantioresolution and Binding Affinity Studies on Human Serum Albumin: Recent Applications and Trends

Thermophoresis for characterizing biomolecular interaction

Chiral Stationary Phases for Liquid Chromatography: Recent Developments

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