Wydział Chemii

Mykhaylo Yu. Losytskyy

Vladyslava B. Kovalska

Oleg A. Varzatskii

Marina V. Kuperman

Sławomir Potocki

Elżbieta Gumienna-Kontecka

Andrey P. Zhdanov

Sergiy M. Yarmoluk

Yan Z. Voloshin

Konstantin Yu. Zhizhin

Nikolai T. Kuznetsov

Anna V. Elskaya

2016

Journal of Luminescence

169

51-60

10.1016/j.jlumin.2015.08.042

Naukowa

Angielski

Artykuł

An interaction of the boron clusterscloso-borates K₂[B₁₀H₁₀], K₂[B₁₂H₁₂] and their functionalized derivatives with serum proteins human (HSA) and bovine (BSA) albumins and immonoglobulin IgG as well as globular proteins β-lactoglobulin and lysozyme was characterized. The steady state and time resolved protein fluorescence quenching studies point on the binding of thecloso-borate arylamine derivatives to serum albumins and discrimination of other proteins. The mechanism of the albumin fluorescence quenching by thecloso-borate arylamine derivatives was proposed. The complex formation between albumin and thecloso-borate molecules has been confirmed by isothermal titration calorimetry (ITC). The compound (K₂[B₁₀H₁₀]) and its arylamine derivative both interact with HSA, have close values ofK_a(1.4 and 1.2×10³M⁻¹respectively) and Gibbs energy (−17.9 and −17.5kJ/mol respectively). However, the arylamine derivative forms complex with the higher guest/host binding ratio (4:1) comparing to the parentcloso-borate (2:1).

Protein fluorescence quenching, Time-resolved fluorescence, Ligand–protein interaction, Closo-borate, Isothermal titration calorimetry

http://dx.doi.org/10.1016/j.jlumin.2015.08.042

http://www.elsevier.com