Affinity capillary electrophoresis is a powerful tool to identify transthyretin binding drugs for potential therapeutic use in amyloidosis

Lorenzi, Ersilia De; Galbusera, Chiara; Bellotti, Vittorio; Mangione, Palma; Massolini, Gabriella; Tabolotti, Elena; Andreola, Alessia; Caccialanza, Gabriele

doi:10.1002/1522-2683(20000901)21:15<3280::aid-elps3280>3.0.co;2-l

Cited by 26 publications

(10 citation statements)

References 40 publications

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“…De Lorenzi et al [88] studied the binding of drugs to the protein transthyretin and determined the affinity constant for thioflavine-transthyretin fibril interactions by CE-FA. Binding to antitrypsin and haptoglobulins has also been probed by CE-FA [71].…”

Section: Binding To Other Proteins and Protein Mixturesmentioning

confidence: 99%

Capillary electrophoresis frontal analysis: Principles and applications for the study of drug‐plasma protein binding

2003

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Capillary electrophoresis frontal analysis: Principles and applications for the study of drug-plasma protein bindingCapillary electrophoresis is a well-established technique for the study of noncovalent interactions. Various approaches exist and capillary electrophoresis-frontal analysis provides an interesting alternative to the migration shift affinity capillary electrophoresis methods and conventional methods. The present work reviews the principles on which the frontal analysis method is founded. Advantages and limitations of capillary electrophoresis frontal analysis in comparison with both conventional and other capillary electrophoresis based methods for quantification of binding interactions are discussed. Investigations utilizing capillary electrophoresis-frontal analysis have focused on the interaction of drugs with plasma proteins. These studies, primarily addressing the binding of drugs to human serum albumin, a 1 -acid glycoprotein, and lipoproteins are reviewed together with some recent developments in capillary electrophoresisfrontal analysis methodology.

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Section: Binding To Other Proteins and Protein Mixturesmentioning

confidence: 99%

Capillary electrophoresis frontal analysis: Principles and applications for the study of drug‐plasma protein binding

2003

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“…The unexpected destabilizing effect of Cu 11 as b 2 -m ligand, favoring fibril formation [24], does not rule out that other ligands could have instead an inhibitory effect on fibril formation, acting as stabilizing agents of the nativelike state of the protein [36,37]. Whereas b 2 -m has a very well determined surface devoted to the interaction with the heavy chain of the class-I major histocompatibility complex [34], it lacks a specific binding site for nonpolypeptidic ligands: a rationale choice of small molecular structures that could bind the protein, as well as the identification of specific functional groups that could be crucial for the protein-drug interaction therefore becomes awkward.…”

Section: Binding To Suraminmentioning

confidence: 99%

Capillary electrophoresis investigation of a partially unfolded conformation of β2-microglobulin

et al. 2002

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Dialysis-related amyloidosis is a disease in which partial unfolding of beta(2)-microglobulin plays a key pathogenetic role in the formation of the amyloid fibrils. We have recently demonstrated that a partially unfolded conformer of beta(2)-microglobulin is involved in fibrillogenesis and that this species is significantly populated under physiological conditions. In this work capillary electrophoresis has been used to measure the equilibrium between the native protein and this conformer in samples known to have a higher or lower amyloidogenic potential, namely full-length beta(2)-microglobulin, two truncated species and a mutant, created by replacing histidine in position 31 with thyrosine. In addition, for all protein species folding stability experiments have been carried out by monitoring the secondary structure by circular dichroism at increasing concentrations of guanidinium chloride. The values of free energy of unfolding in the absence of denaturant, obtained by elaboration of these experiments, were found to be inversely correlated to the area percent of the partially unfolded conformer, as measured by capillary electrophoresis. Affinity capillary electrophoresis experiments have been also carried out under nondenaturing conditions to assess the affinity of copper and suramin to either the native form or the conformational intermediate of full-length beta(2)-microglobulin.

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“…This interaction was characterized by ACE [88]. Other protein-drug interactions, such as cyclophilin-cyclosporin A (an immunosuppressive drug) [89], and, (wild-type transthyretin)-(a pool of drug) [90] binding systems have been studied by CE.…”

Section: Protein-small Molecule Interactionmentioning

confidence: 99%

Recent advances in the study of biomolecular interactions by capillary electrophoresis

Ding

et al. 2004

Electrophoresis

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Recent advances in the study of biomolecular interactions by capillary electrophoresisCapillary electrophoresis (CE) has been abundantly used in the study of molecular interactions owing to such advantages as short analysis time, low sample size requirement, high separation efficiency, and flexible applications. The focus of this paper is to review recent studies and advances (mainly from 1998 to now) in biomolecular interactions using CE. Five CE modes: zone migration CE, affinity CE, frontal analysis (FA), Hummel-Dreyer (HD) and vacancy peak (VP) are cited and compared. Quantitative aspects of the thermodynamics and kinetics of biomolecular interaction are reviewed. Several biomolecular binding systems, including protein-protein (polypeptide), protein-DNA (RNA), protein(polypeptide)-carbohydrate, protein-small molecule, DNAsmall molecule, small molecule-small molecule, have been well characterized by CE. CE is shown to be a powerful tool for the determination of the binding parameters of various bioaffinity interactions.

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Affinity capillary electrophoresis is a powerful tool to identify transthyretin binding drugs for potential therapeutic use in amyloidosis

Cited by 26 publications

References 40 publications

Capillary electrophoresis frontal analysis: Principles and applications for the study of drug‐plasma protein binding

Capillary electrophoresis frontal analysis: Principles and applications for the study of drug‐plasma protein binding

Capillary electrophoresis investigation of a partially unfolded conformation of β2-microglobulin

Recent advances in the study of biomolecular interactions by capillary electrophoresis

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