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Molecules 2016, 21(12), 1706; doi:10.3390/molecules21121706

Interactions of Bovine Serum Albumin with Anti-Cancer Compounds Using a ProteOn XPR36 Array Biosensor and Molecular Docking

1
Academy of Integrative Medicine, Fujian University of Traditional Chinese Medicine, Fuzhou 350122, China
2
Fujian Key Laboratory of Integrative Medicine on Geriatrics, Fujian University of Traditional Chinese Medicine, Fuzhou 350122, China
3
Mengchao Hepatobiliary Hospital of Fujian Medical University, Fuzhou 350025, China
*
Author to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 14 October 2016 / Revised: 28 November 2016 / Accepted: 30 November 2016 / Published: 10 December 2016
(This article belongs to the Section Medicinal Chemistry)
View Full-Text   |   Download PDF [3883 KB, uploaded 23 December 2016]   |  

Abstract

The aim of the work was to determine the interactions of a set of anti-cancer compounds with bovine serum albumin (BSA) using a ProteOn XPR36 array biosensor and molecular docking studies. The results revealed that a total of six anti-cancer compounds: gallic acid, doxorubicin, acteoside, salvianolic acid B, echinacoside, and vincristine were able to reversibly bind to the immobilized BSA. The sensorgrams of these six compounds were globally fit to a Langmuir 1:1 interaction model for binding kinetics analysis. There were significant differences in their affinity for BSA, with doxorubicin, the weakest binding compound having 1000-fold less affinity than salvianolic acid B, the strongest binding compound. However, compounds with a similar KD often exhibited markedly different kinetics due to the differences in ka and kd. Molecular docking experiments demonstrated that acteoside was partially located within sub-domain IIA of BSA, whereas gallic acid bound to BSA deep within its sub-domain IIIA. In addition, the interactions between these compounds and BSA were dominated by hydrophobic forces and hydrogen bonds. Understanding the detailed information of these anti-cancer compounds can provide important insights into optimizing the interactions and activity of potential compounds during drug development. View Full-Text
Keywords: surface plasmon resonance; compounds/BSA interaction; kinetics; molecular docking surface plasmon resonance; compounds/BSA interaction; kinetics; molecular docking
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Zhang, L.; Cai, Q.-Y.; Cai, Z.-X.; Fang, Y.; Zheng, C.-S.; Wang, L.-L.; Lin, S.; Chen, D.-X.; Peng, J. Interactions of Bovine Serum Albumin with Anti-Cancer Compounds Using a ProteOn XPR36 Array Biosensor and Molecular Docking. Molecules 2016, 21, 1706.

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