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Pharmaceutics
Volume 10
Issue 4
10.3390/pharmaceutics10040258
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Article

Importance of Binding Affinity for the Activity of a Metallodendritic Chemical Nuclease

by
Yi-Hsuan Tang
1,
Sodio C. N. Hsu
1,
Po-Yu Chen
1,2,3,
Si-ting Liou
1,
Hui-Ting Chen
4,
Carol Hsin-Yi Wu
5 and
Chai-Lin Kao
1,2,3,*
1
Department of Medicinal and Applied Chemistry, Kaohsiung Medical University, Shih-Chuan 1st Road 100, Kaohsiung 80708, Taiwan
2
Department of Medical Research, Kaohsiung Medical University Hospital, Kaohsiung 80708, Taiwan
3
Department of Chemistry, National Sun Yat-sen University, 70 Lienhai Rd., Kaohsiung 80424, Taiwan
4
Department of Fragrance and Cosmetic Science, Kaohsiung Medical University, Shih-Chuan 1st Road 100, Kaohsiung 80708, Taiwan
5
Division of Cellular and Immune Therapy, Department of Medical Research, Kaohsiung Medical University Hospital, Kaohsiung 80708, Taiwan
*
Author to whom correspondence should be addressed.
Pharmaceutics 2018, 10(4), 258; https://doi.org/10.3390/pharmaceutics10040258
Submission received: 20 October 2018 / Revised: 21 November 2018 / Accepted: 22 November 2018 / Published: 3 December 2018
(This article belongs to the Special Issue Dendrimers in Nanomedical Applications: Update and Future Directions)
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Abstract

A family of bis(2-pyridyl)amino-modified poly(amidoamine) dendrimer Cu complexes was prepared, and their chemical nuclease activities and binding affinity (Kb) levels for DNA plasmid were investigated. The Kb values of the G2 to G6 apodendrimers for DNA plasmid were found to be 7.4, 23, 48, 70, and 280 µM−1, respectively, using ethidium bromide (EtBr) displacement experiments. The chemical nuclease activities of the corresponding complexes were determined by gel electrophoresis, and a clear positive dendritic effect was observed. Further analysis indicated a linear correlation between the Kb values of the G2 to G5 apodendrimers and the nuclease activity of the corresponding complexes. This observation indicated the importance of substrate binding affinity for macromolecular nuclease activity. In addition, an experiment using 3′-(p-hydroxyphenyl) fluorescein suggested that hydroxyl radicals formed under the tested conditions. Subsequently performed inhibition studies indicated that the hydroxyl radical was the active species responsible for the plasmid cleavage.
Keywords: macromolecule nuclease; dendrimers; substrate binding affinity; Cu complexes macromolecule nuclease; dendrimers; substrate binding affinity; Cu complexes
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MDPI and ACS Style

Tang, Y.-H.; Hsu, S.C.N.; Chen, P.-Y.; Liou, S.-t.; Chen, H.-T.; Wu, C.H.-Y.; Kao, C.-L. Importance of Binding Affinity for the Activity of a Metallodendritic Chemical Nuclease. Pharmaceutics 2018, 10, 258. https://doi.org/10.3390/pharmaceutics10040258

AMA Style

Tang Y-H, Hsu SCN, Chen P-Y, Liou S-t, Chen H-T, Wu CH-Y, Kao C-L. Importance of Binding Affinity for the Activity of a Metallodendritic Chemical Nuclease. Pharmaceutics. 2018; 10(4):258. https://doi.org/10.3390/pharmaceutics10040258

Chicago/Turabian Style

Tang, Yi-Hsuan, Sodio C. N. Hsu, Po-Yu Chen, Si-ting Liou, Hui-Ting Chen, Carol Hsin-Yi Wu, and Chai-Lin Kao. 2018. "Importance of Binding Affinity for the Activity of a Metallodendritic Chemical Nuclease" Pharmaceutics 10, no. 4: 258. https://doi.org/10.3390/pharmaceutics10040258

APA Style

Tang, Y.-H., Hsu, S. C. N., Chen, P.-Y., Liou, S.-t., Chen, H.-T., Wu, C. H.-Y., & Kao, C.-L. (2018). Importance of Binding Affinity for the Activity of a Metallodendritic Chemical Nuclease. Pharmaceutics, 10(4), 258. https://doi.org/10.3390/pharmaceutics10040258

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