期刊
BIOORGANIC & MEDICINAL CHEMISTRY
卷 18, 期 23, 页码 8257-8263出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2010.10.005
关键词
Modified nucleosides; RNase A; Agarose gel; Inhibition constant; Docking; PEARLS
资金
- Council of Scientific and Industrial Research (CSIR), India
- Department of Science and Technology (DST), New Delhi, India
Modified nucleosides, molecules, functionalized with various polar groups at different positions have been synthesized to rationalize the impact of structural modification on their inhibitory activity. Agarose gel and precipitation assays indicate their improved inhibitory activity on ribonuclease A (RNase A). Kinetic experiments clearly categorize them as competitive inhibitors of RNase A with improved inhibition constant (K-i) values (37 +/- 9, 67 +/- 6, and 193 +/- 7 mu M for compounds 10, 3, and 7, respectively). The preferential hydrogen bonding network formation between His-12 and His-119 of RNase A with the polar carboxylic and amino groups of these compounds has been evidenced from the docking studies. The relationship between structural modifications and inhibitory activity of these compounds is further justified in terms of energetics using PEARLS. (C) 2010 Elsevier Ltd. All rights reserved.
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