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An Exploration Of Pyrrole Groups On The Enantioselectivity Of Pig Liver Esterase, Brian Long
An Exploration Of Pyrrole Groups On The Enantioselectivity Of Pig Liver Esterase, Brian Long
Honors Theses
Pig Liver Esterase (PLE) is a serine protease enzyme that can interact with one side of a diester to hydrolyze the ester to a carboxylic acid, and research has found that the level of hydrophobicity of side groups can impact the enantioselectivity of PLE hydrolysis.1, 2 The Jones Model is what current researchers use to model the active site of PLE, but the nature of its binding pockets, namely the Hydrophobic Long (HL) pocket, has been called into question.3 Dimethyl 2-((pyrrole-2-yl)methyl)-2-methylmalonate was prepared to be subjected to PLE hydrolysis to see whether enantioselectivity was found. Chiral HPLC revealed 25.32% enantiomeric …
Investigation Of The Effects Of Hydrogen Bonding On The Enantiomeric Excess Of Pig Liver Esterase Hydrolysis Products, Matthew Hasler
Investigation Of The Effects Of Hydrogen Bonding On The Enantiomeric Excess Of Pig Liver Esterase Hydrolysis Products, Matthew Hasler
Honors Theses
Pig Liver Esterase (PLE) is an effective enzyme used in the Masterson Research Group due to its ability to hydrolyze only one ester in a malonic diester. PLE is employed for creating chiral molecules for the synthesis of unnatural amino acid precursors. Previous research in the group found that malonic half esters with hydrogen bonding capable substrates yielded varying degrees of enantiomeric excess, and non-hydrogen bonding substrates yielded racemic mixtures.1,2 The compounds synthesized contained substrates consisting of thiophene rings in the second and third position, and these molecules act as a control for the other research done in the group. …
Investigation Of How Hydrogen Bonding Affects The Enantiomeric Excess Of Pig Liver Esterase Promoted Hydrolysis Of Pro-Chiral Substrates, Jacob E. Pruett
Investigation Of How Hydrogen Bonding Affects The Enantiomeric Excess Of Pig Liver Esterase Promoted Hydrolysis Of Pro-Chiral Substrates, Jacob E. Pruett
Honors Theses
Pig Liver Esterase is a cost effective enzyme for ester hydrolysis. In our group, it is vital for creating chiral molecules for the synthesis of unnatural amino acids of potential biological importance. It has been previously found that the enantiomeric excess (%ee) of the PLE hydrolysis reaction increases drastically with the addition of co-solvents that are able to both accept and donate hydrogen bonds. This research endeavors to see if substrates of enhanced hydrogen bonding ability also increase the stereoselectivity of PLE hydrolyses. Diester malonate was covalently linked with a furan ring in both the third and second position from …