Literature DB >> 9706065

Biexponential decomposition of a neuraminidase inhibitor prodrug (GS-4104) in aqueous solution.

R Oliyai1, L C Yuan, T C Dahl, S Swaminathan, K Y Wang, W A Lee.   

Abstract

PURPOSE: To examine the degradation kinetics and identify the degradation products of a neuraminidase inhibitor prodrug. GS-4104.
METHODS: Degradation was studied as a function of pH and temperature using a stability-indicating RP-HPLC assay. Degradation products were isolated by RP-HPLC and identified by NMR. Specific rate constants were calculated based on a scheme defined by products(s) analysis.
RESULTS: Three distinct degradation products were observed in the pH region studied (pH 2-8): isomer I, GS-4071, and isomer II. Isomer I resulted from the N, N-migration of the acetyl group. Gs-4071 was formed by the hydrolysis of the ethyl ester. Both GS-4071 and isomer I degraded further to isomer II by N, N-acyl migration and ester hydrolysis, respectively. The N, N-acyl migration reaction was characterized using two dimensional heteronuclear multiple bond correlation (HMBC) NMR. The decomposition kinetics of GS-4104 follow a biexponential decay at pH 2-7. The degradation kinetics of Gs-4104 at pH 4.0, 70 degree C were independent of the initial GS-4104 concentration.
CONCLUSIONS: The degradation profile indicates that development of solution or solid dosage from of GS-4104 with adequate shelf-life stability at room temperature is feasible.

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Year:  1998        PMID: 9706065     DOI: 10.1023/a:1011964529805

Source DB:  PubMed          Journal:  Pharm Res        ISSN: 0724-8741            Impact factor:   4.200


  2 in total

1.  Identification of GS 4104 as an orally bioavailable prodrug of the influenza virus neuraminidase inhibitor GS 4071.

Authors:  W Li; P A Escarpe; E J Eisenberg; K C Cundy; C Sweet; K J Jakeman; J Merson; W Lew; M Williams; L Zhang; C U Kim; N Bischofberger; M S Chen; D B Mendel
Journal:  Antimicrob Agents Chemother       Date:  1998-03       Impact factor: 5.191

2.  Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity.

Authors:  C U Kim; W Lew; M A Williams; H Liu; L Zhang; S Swaminathan; N Bischofberger; M S Chen; D B Mendel; C Y Tai; W G Laver; R C Stevens
Journal:  J Am Chem Soc       Date:  1997-01-29       Impact factor: 15.419

  2 in total

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