International Journal of Biological Macromolecules, volume 204, pages 709-717
Effect of ligands with different affinity on albumin fibril formation
Khaibrakhmanova Diliara
1
,
Nikiforova Alena
1
,
Li Ziying
,
Li Zi-Ying
1
,
Sedov Igor A.
2
,
Sedov Igor
Publication type: Journal Article
Publication date: 2022-04-01
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 8.2
ISSN: 01418130, 18790003
Biochemistry
Molecular Biology
General Medicine
Structural Biology
Abstract
The effect of binding of several ligands to bovine serum albumin on the kinetics of fibril formation at denaturing conditions is studied. The considered ligands are clinical drugs with different binding constants to albumin: relatively strong binders (naproxen, ibuprofen, warfarin with 105 to 107 binding constant values) and weak binders (isoniazid, ranitidine with 103 to 104 binding constant values). The data of thioflavin fluorescence binding assay, Congo red binding assay, and circular dichroism spectroscopy indicate ligand concentration-dependent suppression of fibril formation in the presence of strong binders and no effects in the presence of weak binders. Analysis of kinetic curves shows no induction lag associated with fibril nucleation and the first-order kinetics of fibril formation with respect to albumin concentration for all the studied systems. Using DSC method, the fractions of unfolded albumin at incubation temperature were determined for each albumin-ligand system and ligand concentration. Their magnitudes ranging from 0 to 1 correlate with the initial rates of fibril formation and with equilibrium concentrations of fibrils formed in the system after incubation for at least 120 min. The results indicate that fibrils are formed from partially or completely denatured albumin form with the rate proportional to the fraction of this form. Strong albumin binders act as thermodynamic inhibitors of fibrillation shifting the unfolding equilibrium to the side of the native ligand-bound protein.
Citations by journals
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International Journal of Molecular Sciences
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International Journal of Molecular Sciences
1 publication, 25%
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Journal of Molecular Liquids
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Journal of Molecular Liquids
1 publication, 25%
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International Journal of Biological Macromolecules
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International Journal of Biological Macromolecules
1 publication, 25%
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Journal of Molecular Structure
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Journal of Molecular Structure
1 publication, 25%
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Elsevier
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Elsevier
3 publications, 75%
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Multidisciplinary Digital Publishing Institute (MDPI)
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Multidisciplinary Digital Publishing Institute (MDPI)
1 publication, 25%
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Khaibrakhmanova D. et al. Effect of ligands with different affinity on albumin fibril formation // International Journal of Biological Macromolecules. 2022. Vol. 204. pp. 709-717.
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Khaibrakhmanova D., Nikiforova A., Li Z., Li Z., Sedov I., Sedov I. A. Effect of ligands with different affinity on albumin fibril formation // International Journal of Biological Macromolecules. 2022. Vol. 204. pp. 709-717.
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TY - JOUR
DO - 10.1016/j.ijbiomac.2022.01.189
UR - https://doi.org/10.1016%2Fj.ijbiomac.2022.01.189
TI - Effect of ligands with different affinity on albumin fibril formation
T2 - International Journal of Biological Macromolecules
AU - Khaibrakhmanova, Diliara
AU - Nikiforova, Alena
AU - Li, Ziying
AU - Sedov, Igor
AU - Li, Zi-Ying
AU - Sedov, Igor A.
PY - 2022
DA - 2022/04/01 00:00:00
PB - Elsevier
SP - 709-717
VL - 204
SN - 0141-8130
SN - 1879-0003
ER -
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@article{2022_Khaibrakhmanova,
author = {Diliara Khaibrakhmanova and Alena Nikiforova and Ziying Li and Igor Sedov and Zi-Ying Li and Igor A. Sedov},
title = {Effect of ligands with different affinity on albumin fibril formation},
journal = {International Journal of Biological Macromolecules},
year = {2022},
volume = {204},
publisher = {Elsevier},
month = {apr},
url = {https://doi.org/10.1016%2Fj.ijbiomac.2022.01.189},
pages = {709--717},
doi = {10.1016/j.ijbiomac.2022.01.189}
}
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