Abstract
Moffatt oxidation of 2',3'-O-isopropylidene-L-adenosine and treatment of the resulting crude 5'-aldehyde with hydroxylamine followed by deprotection gave L-adenosine 5'-carboxaldehyde oximes, whose enantiomers are known to be potent inhibitors of S-adenosyl-L-homocysteine (AdoHcy) hydrolase. The L-adenosine and its 5'-aldehyde oxime derivatives were found to be inactive as inhibitors of AdoHcy hydrolase. Docking calculations showed that binding of L-adenosine to AdoHcy hydrolase is weaker (higher energy) and less specific (larger number of clusters) compared to D-Ado.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Adenosine / analogs & derivatives*
-
Adenosine / chemical synthesis
-
Adenosine / chemistry*
-
Adenosylhomocysteinase / antagonists & inhibitors
-
Adenosylhomocysteinase / chemistry*
-
Anti-HIV Agents / chemical synthesis
-
Anti-HIV Agents / chemistry
-
Antiviral Agents / chemical synthesis
-
Antiviral Agents / chemistry*
-
Binding Sites
-
Computer Simulation
-
Hepatitis B virus
-
Models, Molecular
-
Oximes / chemical synthesis
-
Oximes / chemistry*
-
Stereoisomerism
-
Structure-Activity Relationship
-
Substrate Specificity
-
Thermodynamics
Substances
-
Anti-HIV Agents
-
Antiviral Agents
-
Oximes
-
Adenosylhomocysteinase
-
Adenosine