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Open AccessArticle

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
Molecules 2016, 21(12), 1706; https://doi.org/10.3390/molecules21121706
Received: 14 October 2016 / Revised: 28 November 2016 / Accepted: 30 November 2016 / Published: 10 December 2016
(This article belongs to the Section Medicinal Chemistry)
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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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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