Article details

Biotechnology and Food Science
Volume 77 Number 1
Experimental and theoretical investigation of drotaverine binding to bovine serum albumin

Krystian Gałęcki1, Gastón Courtade2, Aisling McFall3, Renata Prieschl Teixeira4, Maja Grgic5, Marta Esteve-Sisteré6, Rikke Maglemose Westphalen7, Agnieszka Kowalska-Baron1*
1 Institute of General Food Chemistry, Lodz University of Technology, 90-924 Lodz, Poland
2 Norwegian University of Science and Technology, 7491 Trondheim, Norway
3 Queens University Belfast, BT7 1NN, Northern Ireland
4 Universidade Federal de São Paulo, 04021-001, São Paulo, Brazil
5 Josip Juraj Strossmayer University of Osijek, 31000, Osijek, Croatia
6 ETSEA-University of Lleida, 25198 Lleida, Spain
7 Technical University of Denmark, 2800 KongensLyngby, Denmark


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Pages: 25-36

This study was motivated by the need to provide more insight into the possible mechanism of the intermolecular interactions between antispasmodic drug drotaverine and one of the serum albumins (BSA), with the aim to indicate the most probable sites of these interactions. For this purpose both experimental (spectrofluorometric titration at various temperatures) and theoretical (molecular mechanics) methods have been applied. The obtained results clearly showed that drotaverine quenched BSA fluorescence, and the most probable mechanism is static quenching. The negative value of the theoretically predicted binding free Gibbs energy (-23.8 kJ/mol) confirmed the existence of the intermolecular interactions involving drotaverine and one tryptophan within BSA protein and was well agreed with the experimentally determined value of -25.2 kJ/mol.

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bovine serum albumin, drotaverine, fluorescence quenching, phosphorescence, molecular docking
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