scholarly journals Fluorescence of the tri-cyclic adenine and isoguanine derivatives and their ribosides: possible analytical applications

2019 ◽  
Author(s):  
Alicja Stachelska-Wierzchowska ◽  
Jacek Wierzchowski
Keyword(s):  
Human Blood ◽  
Purine Nucleoside Phosphorylase ◽  
Purine Nucleoside ◽  
Nucleoside Phosphorylase ◽  
Purine Analogs ◽  
Analytical Applications ◽  
Free Media ◽  
Derivatives Of

Fluorescent tri-cyclic purine analogs, derivatives of isoguanine and adenine, were examined as potential substrates of purine-nucleoside phosphorylase. It was found previously that etheno- derivatives of both compounds are ribosylated in phosphate-free media, but ribosylation places in some instances differ from purine N9. New ribosides are examined as potential substrates of human blood PNP and indicators of this enzyme. Of these, N6-riboside of 1,N6-etheno-adenine was found the most promising.

Structure-based design of inhibitors of purine nucleoside phosphorylase. 2. 9-Alicyclic and 9-heteroalicyclic derivatives of 9-deazaguanine

1993 ◽  
Vol 36 (13) ◽  
pp. 1847-1854 ◽  
Author(s):  
John A. Secrist ◽  
Shri Niwas ◽  
Jerry D. Rose ◽  
Y. Sudhakar Babu ◽  
Charles E. Bugg ◽  
...  
Keyword(s):  
Purine Nucleoside Phosphorylase ◽  
Purine Nucleoside ◽  
Nucleoside Phosphorylase ◽  
Derivatives Of

Structure-based design of inhibitors of purine nucleoside phosphorylase. 1. 9-(Arylmethyl) derivatives of 9-deazaguanine

1993 ◽  
Vol 36 (1) ◽  
pp. 55-69 ◽  
Author(s):  
John A. Montgomery ◽  
Shri Niwas ◽  
Jerry D. Rose ◽  
John A. Secrist ◽  
Y. Sudhakar Babu ◽  
...  
Keyword(s):  
Purine Nucleoside Phosphorylase ◽  
Purine Nucleoside ◽  
Nucleoside Phosphorylase ◽  
Derivatives Of

Structure-based design of inhibitors of purine nucleoside phosphorylase. 3. 9-Arylmethyl derivatives of 9-deazaguanine substituted on the arylmethyl group

1993 ◽  
Vol 36 (24) ◽  
pp. 3771-3783 ◽  
Author(s):  
Mark D. Erion ◽  
Shri Niwas ◽  
Jerry D. Rose ◽  
Subramaniam Ananthan ◽  
Mark Allen ◽  
...  
Keyword(s):  
Purine Nucleoside Phosphorylase ◽  
Purine Nucleoside ◽  
Nucleoside Phosphorylase ◽  
Derivatives Of

scholarly journals Some inhibitors of purine nucleoside phosphorylase

2011 ◽  
Vol 57 (5) ◽  
pp. 526-534 ◽  
Author(s):  
L.H. Pogosian ◽  
L.S. Nersesova ◽  
M.G. Gazariants ◽  
Z.S. Mkrtchian ◽  
J.I. Akopian
Keyword(s):  
Purine Nucleoside Phosphorylase ◽  
Cell Metabolism ◽  
Purine Nucleoside ◽  
Heterocyclic Base ◽  
Nucleoside Phosphorylase ◽  
Leading Role ◽  
Tumor Tissues ◽  
T Cell Immunodeficiency ◽  
Synthetic Derivatives ◽  
Derivatives Of

Purine nucleoside phosphorylase (PNP) catalyzes reversible phosphorolysis of purine deoxy- and ribonucleosides with formation (d)Rib-1-P and corresponding bases. PNP plays a leading role in the cell metabolism of nucleosides and nucleotides, as well as in maintaining the immune status of an organism. The major aim of the majority of studies on the PNP is the detection of highly effective inhibitors of this enzyme, derivatives of purine nucleosides used in medicine as immunosuppressors, which are essential for creating selective T-cell immunodeficiency in a human body for organ and tissue transplantation.The present work is devoted to the study of the effects of some synthetic derivatives of purine nucleosides on activity of highly purified PNP from rabbit spleen and also from human healthy and tumor tissues of lung and kidneys. Purine nucleoside analogues modified at various positions of both the heterocyclic base and carbohydrate residues have been investigated. Several compounds, including 8-mercapto-acyclovir, 8-bromo-9-(3,4-hydroxy-butyl)guanine, which demonstrated potent PNP inhibition, could be offered for subsequent study as immunosuppressors during organ and tissue transplantation.

Inhibition of human purine nucleoside phosphorylase by tenofovir phosphate congeners

2010 ◽  
Vol 75 (12) ◽  
pp. 1249-1257 ◽  
Author(s):  
Ivan Votruba ◽  
Jana Trýznová ◽  
Petra Břehová ◽  
Eva Tloušťová ◽  
Květoslava Horská ◽  
...  
Keyword(s):  
Mixed Type ◽  
Purine Nucleoside Phosphorylase ◽  
Docking Studies ◽  
Purine Nucleoside ◽  
Nucleoside Phosphorylase ◽  
Purine Bases ◽  
Structure Activity ◽  
Derivatives Of

The structure-activity study on the phosphates of phosphonomethoxypropyl derivatives of purine bases interacting with human purine nucleoside phosphorylase has shown that the most efficient inhibitors of the enzyme are (R)- and (S)-PMPGp with Ki ~ 1.9 × 10–8 and/or 2.2 × 10–8 mol/l. The kinetic experiments have proven, with the exception of both enantiomers of PMP-8-BrDAPp, strictly competitive character of inhibition for all ANP monophosphates tested. Bromine derivatives exhibited uncompetitive and mixed type of inhibition as well. These results were confirmed by docking studies. The substitution of purine moiety with the bromine at the position 8 lead to an allosteric binding of these compounds toward the enzyme.

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