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Molecules 2015, 20(9), 16491-16523; doi:10.3390/molecules200916491

Spectroscopic Study on the Interaction between Naphthalimide-Polyamine Conjugates and Bovine Serum Albumin (BSA)

Institute of Chemical Biology, Henan University, Kaifeng 475004, China
The Key Laboratory of Natural Medicine and Immuno-Engineering, Henan University, Kaifeng 475004, China
School of Pharmaceutical Sciences, Sun Yat-Sen University, Guangzhou 510006, China
Huaihe Clinical Institute, Henan University, Kaifeng 475004, China
These authors contributed equally to this work.
Authors to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 13 July 2015 / Revised: 14 August 2015 / Accepted: 14 August 2015 / Published: 11 September 2015
(This article belongs to the Section Molecular Diversity)


The effect of a naphthalimide pharmacophore coupled with diverse substituents on the interaction between naphthalimide-polyamine conjugates 14 and bovine serum albumin (BSA) was studied by UV absorption, fluorescence and circular dichroism (CD) spectroscopy under physiological conditions (pH = 7.4). The observed spectral quenching of BSA by the compounds indicated that they could bind to BSA. Furthermore, caloric fluorescent tests revealed that the quenching mechanisms of compounds 13 were basically static type, but that of compound 4 was closer to a classical type. The Ksv values at room temperature for compound-BSA complexes-1-BSA, 2-BSA, 3-BSA and 4-BSA were 1.438 × 104, 3.190 × 104, 5.700 × 104 and 4.745 × 105, respectively, compared with the value of MINS, 2.863 × 104 at Ex = 280 nm. The obtained quenching constant, binding constant and thermodynamic parameter suggested that the binding between compounds 14 with BSA protein, significantly affected by the substituted groups on the naphthalene backbone, was formed by hydrogen bonds, and other principle forces mainly consisting of charged and hydrophobic interactions. Based on results from the analysis of synchronous three-dimensional fluorescence and CD spectra, we can conclude that the interaction between compounds 14 and BSA protein has little impact on the BSA conformation. Calculated results obtained from in silico molecular simulation showed that compound 1 did not prefer either enzymatic drug sites I or II over the other. However, DSII in BSA was more beneficial than DSI for the binding between compounds 24 and BSA protein. The binding between compounds 13 and BSA was hydrophobic in nature, compared with the electrostatic interaction between compound 4 and BSA. View Full-Text
Keywords: naphthalimide-polyamine; conjugates; bovine serum albumin (BSA); spectroscopic methods; molecular docking naphthalimide-polyamine; conjugates; bovine serum albumin (BSA); spectroscopic methods; 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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MDPI and ACS Style

Tian, Z.-Y.; Song, L.-N.; Zhao, Y.; Zang, F.-L.; Zhao, Z.-H.; Chen, N.-H.; Xu, X.-J.; Wang, C.-J. Spectroscopic Study on the Interaction between Naphthalimide-Polyamine Conjugates and Bovine Serum Albumin (BSA). Molecules 2015, 20, 16491-16523.

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