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INTRAMOLECULAR REMOTE FUNCTIONALIZATION OF STEROIDS BY BENZOPHENONE - INCREASED SPECIFICITY BY SOLVENT-INDUCED HYDROPHOBIC INTERACTIONS

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Title INTRAMOLECULAR REMOTE FUNCTIONALIZATION OF STEROIDS BY BENZOPHENONE - INCREASED SPECIFICITY BY SOLVENT-INDUCED HYDROPHOBIC INTERACTIONS
 
Creator LALA, AK
GOKHALE, AP
 
Subject c-h bonds
conformational probes
functionalization
conversion
oxidation
cholestanol
cholesterol
bilayers
membrane
chains
cholesterol
benzophenone
remote functionalization
enzyme model
hydrophobic interactions
 
Description Proximity of reactant sites is one of the major factors that contributes to specificity and high reaction rates observed in enzyme catalysis. Enzymes achieve this proximity between the reactant sites by having high affinity for the substrate. Structural studies on enzyme-substrate complexes provide sufficient evidence in this context and indicate that weak bonding interaction are involved in formation of such complexes. We have exploited the hydrophobic interaction between cholesterol and benzophenone to carry out photoinduced remote functionalisation of cholesterol at specific sites. Thus, using polar solvents intramolecular hydrophobic interaction between cholesterol and benzophenone permitted exclusive functionalisation of ring D in cholesterol. The current study indicates that weak interactions between the reactants can be used to bring them in proximity and photochemical reactions can provide the method for functionalising even inert sites like C-H bonds.
 
Publisher INDIAN ACADEMY SCIENCES
 
Date 2011-08-02T04:14:24Z
2011-12-26T12:53:41Z
2011-12-27T05:40:33Z
2011-08-02T04:14:24Z
2011-12-26T12:53:41Z
2011-12-27T05:40:33Z
1994
 
Type Article
 
Identifier PROCEEDINGS OF THE INDIAN ACADEMY OF SCIENCES-CHEMICAL SCIENCES, 106(5), 971-981
0253-4134
http://dspace.library.iitb.ac.in/xmlui/handle/10054/8656
http://hdl.handle.net/10054/8656
 
Language en