Effect of pH on Albumin Binding with Hydrophobic Porphyrins
- 作者: Lebedeva N.1, Yurina E.1, Gubarev Y.1, Syrbu S.2
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隶属关系:
- Krestov Institute of Solution Chemistry
- Ivanovo State University of Chemistry and Technology
- 期: 卷 89, 编号 3 (2019)
- 页面: 565-569
- 栏目: Article
- URL: https://journals.rcsi.science/1070-3632/article/view/222823
- DOI: https://doi.org/10.1134/S1070363219030368
- ID: 222823
如何引用文章
详细
The behavior of bovine serum albumin as a function of the pH of the medium and the presence in the test systems of symmetrical and asymmetrical hydrophobic porphyrins was investigated. It was established that 4-[(tert-butoxycarbonylamino)acetamido]phenyl group favors stronger protein binding to porphyrin, and this effect enhances in an alkaline medium. Solubilization of protein by porphyrins leads to the fact that the particles are spherical in solution, the hydrodynamic radius of the protein globule reduced in an alkaline medium but in neutral medium, in contrast, increases. By IR spectroscopy it was shown that beta-structuring and the proportion of disordered coils of the polypeptide chain in an alkaline medium increases, because the complexability of the protein towards porphyrin is changes.
作者简介
N. Lebedeva
Krestov Institute of Solution Chemistry
编辑信件的主要联系方式.
Email: nsl@isc-ras.ru
俄罗斯联邦, ul. Akademicheskaya 1, Ivanovo, 153040
E. Yurina
Krestov Institute of Solution Chemistry
Email: syrbu@isuct.ru
俄罗斯联邦, ul. Akademicheskaya 1, Ivanovo, 153040
Yu. Gubarev
Krestov Institute of Solution Chemistry
Email: syrbu@isuct.ru
俄罗斯联邦, ul. Akademicheskaya 1, Ivanovo, 153040
S. Syrbu
Ivanovo State University of Chemistry and Technology
编辑信件的主要联系方式.
Email: syrbu@isuct.ru
俄罗斯联邦, pr. Sheremetevskii 7, Ivanovo, 15300
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