Analysis of binding ability of two tetramethylpyridylporphyrins to albumin and its complex with bilirubin; Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy; Vol. 168

Analysis of binding ability of two tetramethylpyridylporphyrins to albumin and its complex with bilirubin; Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy; Vol. 168

Bibliographic Details
Parent link:Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
Vol. 168.— 2016.— [P. 15-20]
Corporate Author: Национальный исследовательский Томский политехнический университет Управление проректора по научной работе и инновациям Центр RASA в Томске Лаборатория новых лекарственных форм
Other Authors: Solomonov A. V., Shipitsyna M. K., Rumyantsev E. V., Timin A. S. Aleksandr Sergeevich, Ivanov S. P. Sergey Pavlovich, Vashurin A. S.
Summary:Title screen
An interaction between 5,10,15,20-tetrakis-(N-methyl-x-pyridyl)porphyrins, x = 2; 4 (TMPyPs) with bovine serum albumin (BSA) and its bilirubin (BR) complex was investigated by UV–Viz and fluorescence spectroscopy under imitated physiological conditions involving molecular docking studies. The parameters of forming intermolecular complexes (binding constants, quenching rate constants, quenching sphere radius etc.) were determined. It was showed that the interaction between proteins and TMPyPs occurs via static quenching of protein fluorescence and has predominantly hydrophobic and electrostatic character. It was revealed that obtained complexes are relatively stable, but in the case of TMPyP4 binding with proteins occurs better than TMPyP2. Nevertheless, both TMPyPs have better binding ability with free protein compared to BRBSA at the same time. The influence of TMPyPs on the conformational changes in protein molecules was studied using synchronous fluorescence spectroscopy. It was found that there is no competition of BR with TMPyPs for binging sites on protein molecule and BR displacement does not occur. Molecular docking calculations have showed that TMPyPs can bind with albumin via tryptophan residue in the hydrophilic binding site of protein molecule but it is not one possible interaction way.
Режим доступа: по договору с организацией-держателем ресурса
Language:English
Published: 2016
Subjects:
электронный ресурс
труды учёных ТПУ
спектроскопия
межмолекулярные взаимодействия
Online Access:http://dx.doi.org/10.1016/j.saa.2016.05.044
Format: Electronic Book Chapter
KOHA link:https://koha.lib.tpu.ru/cgi-bin/koha/opac-detail.pl?biblionumber=650342

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