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Open AccessArticle

Analysis of Binding Interactions of Ramipril and Quercetin on Human Serum Albumin: A Novel Method in Affinity Evaluation

1
Department of Pharmacognosy and Botany, Faculty of Pharmacy, Comenius University in Bratislava, 83232 Bratislava, Slovakia
2
Department of Physical Chemistry of Drugs, Faculty of Pharmacy, Comenius University in Bratislava, 83232 Bratislava, Slovakia
3
Institute of Biophysics, Department of Nanobiotechnology, University of Natural Resources and Life Sciences, 1180 Vienna, Austria
4
Institute of Biochemistry, Department of Chemistry, University of Natural Resources and Life Sciences, 1180 Vienna, Austria
*
Author to whom correspondence should be addressed.
Molecules 2020, 25(3), 547; https://doi.org/10.3390/molecules25030547
Received: 8 January 2020 / Revised: 21 January 2020 / Accepted: 25 January 2020 / Published: 27 January 2020
The aim of this study was to analyze the binding interactions between a common antihypertensive drug (ramipril, R) and the widely distributed plant flavonoid quercetin (Q), in the presence of human serum albumin (HSA). From the observed fluorescence spectra of the (HSA + R) system we can assume that ramipril is also one of the Site 3 ligands—similar to fusidic acid—the binding of which has been proven by RTG crystallography. Our claim is supported by near-UV CD spectroscopy, microscale themophoresis and molecular modeling. The presence of R slightly inhibited the subsequent binding of Q to HSA and, on the contrary, the pre-incubation of HSA with Q caused a stronger binding of R, most likely due to allosteric interactions. At high concentrations, R is also able to displace Q from its binding site. The dissociation constant KD for the binding of R is more than hundredfold larger than for Q, which means that R is a very weak binder to HSA. The knowledge of qualitative and quantitative parameters of R, as well as the methods used in this study, are important for future research into HSA binding. This study shows the importance of implementing other methods for KD determination. Microscale thermophoresis has proved to be a novel, practical and accurate method for KD determination on HSA, especially in cases when fluorescence spectroscopy is unable to produce usable results. View Full-Text
Keywords: human serum albumin; ramipril; quercetin; fluorescence; microscale thermophoresis; circular dichroism; molecular docking human serum albumin; ramipril; quercetin; fluorescence; microscale thermophoresis; circular dichroism; molecular docking
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Vaneková, Z.; Hubčík, L.; Toca-Herrera, J.L.; Furtműller, P.G.; Mučaji, P.; Nagy, M. Analysis of Binding Interactions of Ramipril and Quercetin on Human Serum Albumin: A Novel Method in Affinity Evaluation. Molecules 2020, 25, 547.

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