© 2020 Elsevier B.V. There is a demand in rapid and robust methods to determine the affinity of drugs to receptors, enzymes, and transport proteins. Differential scanning calorimetry (DSC) is a common method to prove the existence of ligand–protein binding from the shift of denaturation peak, but it is rarely used to obtain the binding constant values. The work is aimed to prove that the DSC experiments can be a source of reliable values of the binding constants and information on the stoichiometry of drug-albumin binding. DSC thermograms of bovine serum albumin denaturation in the presence of several drugs with different affinity and stoichiometry of binding to albumin: naproxen, warfarin, ibuprofen, and isoniazid were recorded. The depend...
This work analyzed the thermal denaturation process of defatted bovine serum albumin (BSA). DSC meas...
Human serum albumin possesses multiple binding sites and transports a wide range of ligands that inc...
The drug-human serum albumin binding interaction was evaluated on a stationary phase immobilized wit...
The DSC technique is applied for quantification of the thermodynamic binding constants in protein-li...
This paper describes an expanded application of our recently reported method (Eskew et al., Analytic...
Understanding physical chemistry underlying drug-protein interactions is essential to devise guideli...
A quantitative understanding of the mode of interaction of drugs with target proteins provides a gui...
Binding of the drugs naproxen (which is an anti-inflammatory) and amitriptyline (which is an anti-de...
The dataset contains literature values of the experimental equilibrium binding constants of drugs an...
Human serum albumin (HSA) is the most abundant human plasma protein. HSA plays a crucial role in man...
A dataset containing the experimental values of the equilibrium binding constants of clinical drugs,...
Screening of ligands that can bind to biologic products of in vitro expression systems typically req...
Introduction High sensitive Differential scanning calorimetry (DSC) is the only technique giving di...
Human serum albumin (HSA) is a soluble protein in our circulatory system, which is known to bind a v...
An understanding of the detailed energetics and mechanism of the binding of drugs with target protei...
This work analyzed the thermal denaturation process of defatted bovine serum albumin (BSA). DSC meas...
Human serum albumin possesses multiple binding sites and transports a wide range of ligands that inc...
The drug-human serum albumin binding interaction was evaluated on a stationary phase immobilized wit...
The DSC technique is applied for quantification of the thermodynamic binding constants in protein-li...
This paper describes an expanded application of our recently reported method (Eskew et al., Analytic...
Understanding physical chemistry underlying drug-protein interactions is essential to devise guideli...
A quantitative understanding of the mode of interaction of drugs with target proteins provides a gui...
Binding of the drugs naproxen (which is an anti-inflammatory) and amitriptyline (which is an anti-de...
The dataset contains literature values of the experimental equilibrium binding constants of drugs an...
Human serum albumin (HSA) is the most abundant human plasma protein. HSA plays a crucial role in man...
A dataset containing the experimental values of the equilibrium binding constants of clinical drugs,...
Screening of ligands that can bind to biologic products of in vitro expression systems typically req...
Introduction High sensitive Differential scanning calorimetry (DSC) is the only technique giving di...
Human serum albumin (HSA) is a soluble protein in our circulatory system, which is known to bind a v...
An understanding of the detailed energetics and mechanism of the binding of drugs with target protei...
This work analyzed the thermal denaturation process of defatted bovine serum albumin (BSA). DSC meas...
Human serum albumin possesses multiple binding sites and transports a wide range of ligands that inc...
The drug-human serum albumin binding interaction was evaluated on a stationary phase immobilized wit...