Investigation of the Interaction Between Human Serum Albumin and Two Drugs as Binary and Ternary Systems

European Journal of Drug Metabolism and Pharmacokinetics
Nooshin AbdollahpourJ Chamani

Abstract

Human serum albumin (HSA) is the most frequent protein in blood plasma. Albumin transports various compounds, preserves osmotic pressure, and buffers pH. A unique feature of albumin is its ability to bind drugs and other bioactive molecules. However, it is important to consider binary and ternary systems of two pharmaceuticals to estimate the effect of the first drug on the second one and physicochemical properties. Different techniques including time-resolved, second-derivative and anisotropy fluorescence spectroscopy, resonance light scattering (RLS), critical induced aggregation concentration (C CIAC), particle size, zeta potential and stability analysis were employed in this assessment to elucidate the binding behavior of Amlodipine and Aspirin to HSA. Moreover, isothermal titration calorimetric techniques were performed and the QSAR properties were applied to analyze the hydration energy and log P. Multiple sequence alignments were also used to predict the structure and biological characteristics of the HSA binding site. Time-resolved fluorescence spectroscopy showed interaction of both drugs to HSA based on a static quenching mechanism. Subsequently, second-derivative fluorescence spectroscopy presented different values o...Continue Reading

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Oct 16, 2018·Expert Opinion on Drug Discovery·Michael RonzettiAnton Simeonov
Jul 28, 2018·Journal of Biomolecular Structure & Dynamics·Hamid TanzadehpanahMassoud Saidijam
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