Next Article in Journal
Immobilization of Horseradish Peroxidase on NH2-Modified Magnetic Fe3O4/SiO2 Particles and Its Application in Removal of 2,4-Dichlorophenol
Previous Article in Journal
A Multi-Scale Computational Study on the Mechanism of Streptococcus pneumoniae Nicotinamidase (SpNic)
Article Menu
Issue 10 (October) cover image

Export Article

Open AccessArticle
Molecules 2014, 19(10), 15754-15767; doi:10.3390/molecules191015754

Design, Synthesis and SAR Studies of NAD Analogues as Potent Inhibitors towards CD38 NADase

1
State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, Beijing 100191, China
2
School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen 518052, China
*
Author to whom correspondence should be addressed.
Received: 25 July 2014 / Revised: 22 September 2014 / Accepted: 22 September 2014 / Published: 29 September 2014
(This article belongs to the Section Medicinal Chemistry)
View Full-Text   |   Download PDF [825 KB, uploaded 29 September 2014]   |  

Abstract

Nicotinamide adenine dinucleotide (NAD), one of the most important coenzymes in the cells, is a substrate of the signaling enzyme CD38, by which NAD is converted to a second messenger, cyclic ADP-ribose, which releases calcium from intracellular calcium stores. Starting with 2′-deoxy-2′-fluoroarabinosyl-β-nicotinamide adenine dinucleotide (ara-F NAD), a series of NAD analogues were synthesized and their activities to inhibit CD38 NAD glycohydrolase (NADase) were evaluated. The adenosine-modified analogues showed potent inhibitory activities, among which 2′-deoxy-2′-fluoroarabinosyl-β-nicotinamide guanine dinucleotide (ara-F NGD) was the most effective one. The structure-activity relationship of NAD analogues was also discussed. View Full-Text
Keywords: synthesis; NAD analogues; CD38; inhibitors synthesis; NAD analogues; CD38; inhibitors
Figures

Figure 1

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).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Wang, S.; Zhu, W.; Wang, X.; Li, J.; Zhang, K.; Zhang, L.; Zhao, Y.-J.; Lee, H.C.; Zhang, L. Design, Synthesis and SAR Studies of NAD Analogues as Potent Inhibitors towards CD38 NADase. Molecules 2014, 19, 15754-15767.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top