scholarly journals Synthesis and Preliminary Evaluation of Biological Activity of Glycoconjugates Analogues of Acyclic Uridine Derivatives

Molecules ◽  
2018 ◽  
Vol 23 (8) ◽  
pp. 2017 ◽  
Author(s):  
Roman Komor ◽  
Gabriela Pastuch-Gawolek ◽  
Ewelina Krol ◽  
Wieslaw Szeja

Herein we present the methodology for obtaining glycosyltransferase inhibitors, analogues of natural enzyme substrates of donor-type: UDP-glucose and UDP-galactose. The synthesis concerned glycoconjugates, nucleoside analogues containing an acyclic ribose mimetic linked to a uracil moiety in their structure. The biological activity of the synthesised compounds was determined on the basis of their ability to inhibit the model enzyme action of β-1,4-galactosyltransferase from bovine milk. The obtained results allowed to expand and supplement the existing library of synthetic compounds that are able to regulate the biological activity of enzymes from the GT class.

2019 ◽  
Vol 30 (3) ◽  
pp. 27
Author(s):  
D. U. Rajawardana ◽  
I. G. N. Hewajulige ◽  
C. M. Nanayakkara ◽  
S. K. M. R. A. Athurupana ◽  
W. M. T. Madhujith

2015 ◽  
Vol 2015 (9) ◽  
pp. 1505-1510 ◽  
Author(s):  
Wanning Hu ◽  
Jan Hoyer ◽  
Ines Neundorf ◽  
Preshendren Govender ◽  
Gregory S. Smith ◽  
...  

2002 ◽  
Vol 133 (4) ◽  
pp. 499-520 ◽  
Author(s):  
Michael E. Jung ◽  
Akemi Toyota ◽  
Erik de Clercq ◽  
Jan Balzarini

2001 ◽  
Vol 70 (1-2) ◽  
pp. 79-85 ◽  
Author(s):  
K. Sejrsen ◽  
L.O. Pedersen ◽  
M. Vestergaard ◽  
S. Purup

2016 ◽  
Vol 14 (46) ◽  
pp. 10787-10798 ◽  
Author(s):  
David Mangan ◽  
Neasa McNabola ◽  
Emily H. Clark ◽  
Isabel Bermudez ◽  
Susan Wonnacott ◽  
...  

A new synthesis of mecamylamine allowed the preparation of analogues to probe biological activity.


2013 ◽  
Vol 76 (12) ◽  
pp. 2037-2039 ◽  
Author(s):  
STEPHEN E. LUMOR ◽  
BRONWYN D. DEEN ◽  
IAN RONNINGEN ◽  
KENNETH SMITH ◽  
NEAL R. FREDRICKSON ◽  
...  

The effect of lactose at the concentration typically found in milk (134 mM) on the ability of ricin to inhibit protein synthesis in HeLa cells was studied. Ricin (0.001 to 300 μg/ml) that was either not treated or treated with 134 mM lactose was added to test tubes containing 1 ml of HeLa cells (approximately 3 × 105 cells in a low-leucine medium). After 2 h of incubation at 37°C, 0.5 μCi of l-[U-14C]-leucine was added to each tube and incubated for another 60 min. The cells were harvested by centrifugation and lysed, and cellular proteins were separated. The amount of radioactivity incorporated into the proteins was determined by liquid scintillation. The biological activity of ricin, i.e., the amount of radioactivity in a sample relative to that of the control (cells not treated with ricin), was calculated for each treatment. The inhibitory effect of 134 mM lactose on the biological activity of ricin was only significant at concentrations of ricin below 1 μg/ml. At higher ricin concentrations, the effect of 134 mM lactose decreased as the concentration of ricin increased, resulting in an increase in the inhibition of proteins synthesis. Our results also indicated that bovine milk, when used in place of 134 mM lactose, was more effective for reducing the activity of ricin at concentrations below 1 μg/ml but was ineffective against ricin concentrations greater than 1 μg/ml. These results suggest that milk may not protect against ricin intoxication at the concentration (0.89 μg/ml) equivalent to the lowest limit of its 50% lethal dose for a 20-kg child consuming 225 ml (8 oz) of milk.


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