6533b851fe1ef96bd12a8d74
RESEARCH PRODUCT
Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging
Rakesh PuttreddyKäthe M. DahlströmKari RissanenXiang-guo LiXiang-guo LiSaija SirénSaija SirénArto LiljebladTiina A. SalminenMika Scheininsubject
entsyymitaromaattiset yhdisteetbiocatalysisStereochemistryPharmaceutical Sciencemerkkiaineet010402 general chemistry01 natural sciencesArticleAnalytical ChemistryKinetic resolutionlcsh:QD241-441lcsh:Organic chemistryAcyl bindinglipaasitDrug DiscoveryHydrolasekinetic resolutionPhysical and Theoretical ChemistryLipaseBinding sitebiology010405 organic chemistryChemistrymolecular modelingOrganic ChemistryActive sitebiokatalyysiDIBOlipase A from Candida antarcticabiology.organism_classificationlaskennallinen kemialuonnonaineet0104 chemical scienceshiivasienetChemistry (miscellaneous)lipase a from <i>candida antarctica</i>biology.proteinMolecular MedicineCandida antarcticaEnantiomerdescription
The enantiomers of aromatic 4-dibenzocyclooctynol (DIBO), used for radiolabeling and subsequent conjugation of biomolecules to form radioligands for positron emission tomography (PET), were separated by kinetic resolution using lipase A from Candida antarctica (CAL-A). In optimized conditions, (R)-DIBO [(R)-1, ee 95%] and its acetylated (S)-ester [(S)-2, ee 96%] were isolated. In silico docking results explained the ability of CAL-A to differentiate the enantiomers of DIBO and to accommodate various acyl donors. Anhydrous MgCl2 was used for binding water from the reaction medium and, thus, for obtaining higher conversion by preventing hydrolysis of the product (S)-2 into the starting material. Since the presence of hydrated MgCl26H2O also allowed high conversion or effect on enantioselectivity, Mg2+ ion was suspected to interact with the enzyme. Binding site predictions indicated at least two sites of interest
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2020-02-01 | Molecules |