Drugs online research references
Rom J Virol. 1995 Jan-Jun;46(1-2):9-19.
Testing of some pharmacological characteristics of the autochthonous product Acyclovir.
Mutiu A, Belu O, Rojanschi D, Petica M, Crisan I, Vasilioni V, Fodor C.
Stefan Nicolau Institute of Virology, Bucharest, Romania.
In the present work, the preliminary results of a study regarding the pharmacokinetic properties of the autochthonous synthetic drug Acyclovir are shown. The in vitro and in vivo toxicologic test demonstrates a low toxicity of this product, the drug being well tolerated both by the laboratory animal and by the fibroblasts of the human embryo. The specific antiviral action of the product on the multiplication in vitro of the Herpes simplex virus types 1 and 2, appreciated by the lowering capacity of the infection titre and by the determination of the inhibitory concentration 50% (IC50), is significant and comparable with previous results obtained by the authors by testing the drug Zovirax of the Welcome firm.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9106397&dopt=Abstract
J Med Chem. 1995 Sep 15;38(19):3850-6.
Inhibition of uridine phosphorylase: synthesis and structure-activity relationships of aryl-substituted 5-benzyluracils and 1-[(2-hydroxyethoxy)methyl]-5-benzyluracils.
Orr GF, Musso DL, Boswell GE, Kelley JL, Joyner SS, Davis ST, Baccanari DP.
Division of Organic Chemistry, Burroughs Wellcome Co., Research Triangle Park, North Carolina 27709, USA.
A series of 1-[(2-hydroxyethoxy)methyl]-5-benzyluracils were synthesized and tested for inhibition of murine liver uridine phosphorylase (UrdPase). Inhibitors of UrdPase are reported to enhance the chemotherapeutic utility of 5-fluoro-2'-deoxyuridine and 5-fluorouracil and to ameliorate zidovudine-induced anemia in animal models. We prepared a series of 5-aryl-substituted analogues of 5-benzylacyclouridine (BAU), a good inhibitor of UrdPase (IC50 of 0.46 microM), to develop a compound with enhanced potency and improved pharmacokinetics. The first phase of structure-activity relationship studies on a series of 32 aryl-substituted 5-benzyluracils found several 5-(3-alkoxybenzyl) analogues of 5-benzyluracil with enhanced potency. The acyclovir side chain, the (2-hydroxyethoxy)methyl group, was substituted on the more potent aryl-substituted 5-benzyluracils. The two most potent compounds, 10y (3-propoxy) and 10dd (3-sec-butoxy), were inhibitors of UrdPase with IC50s of 0.047 and 0.027 microM, respectively. Six compounds were tested in vivo for effects on steady-state concentrations of circulating uridine in rats. Plasma uridine levels were elevated 3-9-fold by compound levels that ranged from 8 to 50 microM.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7562916&dopt=Abstract
Anal Biochem. 1998 Dec 15;265(2):299-307.
Purine nucleoside phosphorylase: its use in a spectroscopic assay for inorganic phosphate and for removing inorganic phosphate with the aid of phosphodeoxyribomutase.
Nixon AE, Hunter JL, Bonifacio G, Eccleston JF, Webb MR.
National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, UK.
The kinetics of the phosphorolysis of 7-methylated guanosine analogues catalyzed by purine nucleoside phosphorylase has been analyzed to understand the use of this system as a "Pi mop" to remove Pi from solutions and as a spectroscopic assay for Pi at micromolar concentrations. An expression system was developed for the phosphorylase from Escherichia coli: this protein (subunit molecular mass 26 kDa) and one from a commercial source (29 kDa) were used in this study. Rates of >50 s-1 were obtained for the phosphorolysis at 30 degrees C, so that when the phosphorylase is coupled to the phosphatase being studied, rates of Pi release from the phosphatase can be measured close to this rate. The kinetic mechanism appears to obey the Michaelis-Menten model in the steady state with the bond cleavage rate limiting. Slow hydrolysis of ribose-1-phosphate to Pi catalyzed by the phosphorylase limits the efficiency of the Pi mop. To overcome this, phosphodeoxyribomutase was used to catalyze the conversion of ribose-1-phosphate to ribose-5-phosphate, enabling the Pi mop to remove large amounts of Pi quantitatively. Acyclovir diphosphate provides a simple method to switch off the Pi mop as it is a tight inhibitor (Kd 12 nM) of purine nucleoside phosphorylase. Copyright 1998 Academic Press.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9882406&dopt=Abstract
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