106386-45-2

Upstream product

• 91800-98-5 1-(2,2-dibromoethynyl)adamantane 
• 768-90-1 1-Adamantyl bromide 
• 73213-43-1 p-nitrophenyl 1-adamantylpropiolate 
• 124-38-9 carbon dioxide 
• 40430-66-8 1-ethynyladamantane 

Downstream Products

• 129694-12-8 Adamantan-1-yl-propynoic acid 3-chloro-phenyl ester 
• 129694-09-3 Adamantan-1-yl-propynoic acid 2,5-dinitro-phenyl ester 
• 129694-13-9 Adamantan-1-yl-propynoic acid 4-chloro-phenyl ester 
• 129694-15-1 Adamantan-1-yl-propynoic acid 2,4-dimethyl-phenyl ester 
• 187461-69-4 Adamantan-1-yl-propynoic acid 4'-tert-butyl-3-nitro-biphenyl-4-yl ester 
• 129694-14-0 Adamantan-1-yl-propynoic acid phenyl ester 
• 129694-10-6 Adamantan-1-yl-propynoic acid 4-cyano-phenyl ester 
• 129694-11-7 Adamantan-1-yl-propynoic acid 3-nitro-phenyl ester 
• 73213-43-1 p-nitrophenyl 1-adamantylpropiolate 

Relevant academic research and scientific papers

Ester hydrolysis by a catalytic cyclodextrin dimer enzyme mimic with a metallobipyridyl linking group

A β-cyclodextrin dimer with a linking bipyridyl group is synthesized as a catalyst precursor, a holoenzyme mimic. It binds both ends of potential substrates into the two different cyclodextrin cavities, holding the substrate ester carbonyl group directly above a metal ion bound to the bipyridyl unit. The result is very effective ester hydrolysis with good turnover catalysis. For example, a Cu(II) complex accelerates the rate of hydrolysis of several nitrophenyl esters by a factor of 104-105, with at least 50 turnovers and no sign of product inhibition. In the best case, with an added nucleophile that also binds to the metal ion, a rate acceleration of 1.45 x 107 over the background reaction rate was observed. Hydrolysis by a catalyst with only one cyclodextrin binding group is significantly slower than in the bidentate binding cases. As expected, the binding of a transition state analogue to these catalysts is stronger with the metal ion present than without. This and kinetic evidence point to a mechanism in which the metal ion plays a bifunctional acid-base role, enforced by the binding geometry that holds the substrate functionality right on top of the catalytic metal ion.

Improved Acylation Rates within Cyclodextrin Complexes from Flexible Capping of the Cyclodextrin and from Adjustment of the Substrate Geometry

The acylation of β-cyclodextrin by bound substrates has been studied as a model for serine acylase enzymes such as chymotrypsin.Molecular model building suggested that previously examined substrates, which had given acylation rates only a few hundred times accelerated over the hydrolysis rates, were not optimal geometrically.In our work the geometry for such processes has been improved by fashioning an "intrusive floor" on the cyclodextrin cavity, leading to improved rates.Greater improvements have come from substrate modification, using substrates based on the cinnamic acid, adamantane, and ferrocene frameworks.The rates correlate well with the geometric predictions from molecular models.The best case leads to an acceleration of acylation, relative to hydrolysis, of 106-107-fold, exceeding that for chymotrypsin with p-nitrophenyl acetate.