| Title | Synthesis of deuterated-BCX-1777, a potent inhibitor of purine nucleoside phosphorylase |
| Publication Type | Journal Article |
| Year of Publication | 2002 |
| Authors | Kezar III, H. S., Hutchison T. L., Tyler P. C., and Morris Jr. P. E. |
| IRL Team | Carbohydrate Chemistry |
| Journal | Journal of Labelled Compounds and Radiopharmaceuticals |
| Volume | 45 |
| Pagination | 71-78 |
| Keywords | article, Catalysis, chemical bond, Deuterium, drug structure, drug synthesis, immucillin h, mass spectrometry, purine nucleoside phosphorylase inhibitor, unclassified drug |
| Abstract | BCX-1777, a novel inhibitor of the enzyme purine nucleoside phosphorylase, mimics the charged ribosyl oxocarbenium ion formed during the transition state of the enzyme-catalyzed C-N bond cleavage of nucleosides. BCX-1777 is a slow-onset, tight-binding inhibitor with a K1* of 23 pM and is one of the most potent inhibitors known for the enzyme. In support of our BCX-1777 program, a mass spectrometric assay has been developed utilizing 5′-[2H]-BCX-1777 as an internal standard. The synthesis of 5′-[2H]-BCX-1777 is described in this report. Copyright © 2002 John Wiley & Sons, Ltd. |
| URL | http://www.scopus.com/inward/record.url?eid=2-s2.0-0036157739&partnerID=40&md5=e6d060500e35c01106b223f0a196b901 |
| DOI | 10.1002/jlcr.533 |
