An interaction of the functionalized closo-borates with albumins: The protein fluorescence quenching and calorimetry study
An interaction of the functionalized closo-borates with albumins: The protein fluorescence quenching and calorimetry study
复制标题
DOI:
10.1016/j.jlumin.2015.08.042
复制
发表时间:
2016-01-01
影响因子:
3.6
通讯作者:
Elskaya, Anna V.
中科院分区:
文献类型:
--
作者:
Losytskyy, Mykhaylo Yu.;Kovalska, Vladyslava B.;Elskaya, Anna V.
An interaction of the boron clusters closo-borates K-2[B10H10], K-2[B12H12] and their functionalized derivatives with serum proteins human (RSA) and bovine (BSA) albumins and immonoglobulin IgG as well as globular proteins beta-lactoglobulin and lysozyme was characterized. The steady state and time resolved protein fluorescence quenching studies point on the binding of the closo-borate arylamine derivatives to serum albumins and discrimination of other proteins. The mechanism of the albumin fluorescence quenching by the closo-borate arylamine derivatives was proposed.The complex formation between albumin and the closo-borate molecules has been confirmed by isothermal titration calorimetry (ITC). The compound (K-2[B10H10]) and its arylamine derivative both interact with HSA, have close values of K-a (1.4 and 1.2 x 10(3) M-1 respectively) and Gibbs energy (-17.9 and -17.5 kJ/mol respectively). However, the arylamine derivative forms complex with the higher guest/host binding ratio (4:1) comparing to the parent closo-borate (2:1). (C) 2015 Elsevier B.V. All rights reserved.