Analysis of binding ability of two tetramethylpyridylporphyrins to albumin and its complex with bilirubin.
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.
Inorganic Chemistry Department, Ivanovo State University of Chemistry and Technology, 7 Sheremetevskij prosp., 153000 Ivanovo, Russian Federation; Department of Materials and Interfaces, Weizmann Institute of Science, Rehovot 7610001, Israel. Electronic address: Deus-Lex@yandex.ru.
Alexey V
AV
Solomonov
Inorganic Chemistry Department, Ivanovo State University of Chemistry and Technology, 7 Sheremetevskij prosp., 153000 Ivanovo, Russian Federation. Electronic address: higgitown@yandex.ru.
Maria K
MK
Shipitsyna
Inorganic Chemistry Department, Ivanovo State University of Chemistry and Technology, 7 Sheremetevskij prosp., 153000 Ivanovo, Russian Federation. Electronic address: asvashurin@mail.ru.
Arthur S
AS
Vashurin
Inorganic Chemistry Department, Ivanovo State University of Chemistry and Technology, 7 Sheremetevskij prosp., 153000 Ivanovo, Russian Federation. Electronic address: evr@isuct.ru.
Evgeniy V
EV
Rumyantsev
Inorganic Chemistry Department, Ivanovo State University of Chemistry and Technology, 7 Sheremetevskij prosp., 153000 Ivanovo, Russian Federation; Tomsk Polytechnic University, RASA Center in Tomsk, 30, Lenin Avenue, 634500 Tomsk, Russian Federation. Electronic address: a_timin@mail.ru.
Alexander S
AS
Timin
Ufa Institute of Chemistry of the Russian Academy of Sciences, Prosp. Oktyabrya 71, Ufa 450045, Russian Federation. Electronic address: ivanov_sp@anrb.ru.
Sergey P
SP
Ivanov
D000818:Animals; D001663:Bilirubin / Q000031:analogs & derivatives / Q000378:metabolism*; D001665:Binding Sites; D002417:Cattle; D057927:Hydrophobic and Hydrophilic Interactions; D062105:Molecular Docking Simulation; D011166:Porphyrins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D011166:Porphyrins; D012710:Serum Albumin, Bovine; C021096:tetra(4-N-methylpyridyl)porphine; D001663:Bilirubin
Albumin; Bilirubin; Intermolecular interactions; Molecular docking; Pyridylporphyrins; Spectroscopy