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dc.contributor.authorSirén, Saija
dc.contributor.authorDahlström, Käthe M.
dc.contributor.authorPuttreddy, Rakesh
dc.contributor.authorRissanen, Kari
dc.contributor.authorSalminen, Tiina A.
dc.contributor.authorScheinin, Mika
dc.contributor.authorLi, Xiang-Guo
dc.contributor.authorLiljeblad, Arto
dc.date.accessioned2020-02-28T09:33:26Z
dc.date.available2020-02-28T09:33:26Z
dc.date.issued2020
dc.identifier.citationSirén, S., Dahlström, K. M., Puttreddy, R., Rissanen, K., Salminen, T. A., Scheinin, M., Li, X.-G., & Liljeblad, A. (2020). Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging. <i>Molecules</i>, <i>25</i>(4), Article 879. <a href="https://doi.org/10.3390/molecules25040879" target="_blank">https://doi.org/10.3390/molecules25040879</a>
dc.identifier.otherCONVID_34751885
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/68001
dc.description.abstractThe 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; one in the lid domain at the bottom of the acyl binding pocket and another at the interface of the hydrolase and flap domains, just above the active site.en
dc.format.mimetypeapplication/pdf
dc.languageeng
dc.language.isoeng
dc.publisherMDPI
dc.relation.ispartofseriesMolecules
dc.rightsCC BY 4.0
dc.subject.otherbiocatalysis
dc.subject.otherlipase A from Candida antarctica
dc.subject.otherDIBO
dc.subject.otherkinetic resolution
dc.subject.othermolecular modeling
dc.titleCandida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202002282224
dc.contributor.laitosKemian laitosfi
dc.contributor.laitosDepartment of Chemistryen
dc.contributor.oppiaineOrgaaninen kemiafi
dc.contributor.oppiaineOrganic Chemistryen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.description.reviewstatuspeerReviewed
dc.relation.issn1420-3049
dc.relation.numberinseries4
dc.relation.volume25
dc.type.versionpublishedVersion
dc.rights.copyright© 2020 by the authors. Licensee MDPI, Basel, Switzerland.
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber298817
dc.subject.ysoentsyymit
dc.subject.ysoaromaattiset yhdisteet
dc.subject.ysomerkkiaineet
dc.subject.ysolaskennallinen kemia
dc.subject.ysobiokatalyysi
dc.subject.ysolipaasit
dc.subject.ysohiivasienet
dc.subject.ysoluonnonaineet
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p4769
jyx.subject.urihttp://www.yso.fi/onto/yso/p23502
jyx.subject.urihttp://www.yso.fi/onto/yso/p17476
jyx.subject.urihttp://www.yso.fi/onto/yso/p23053
jyx.subject.urihttp://www.yso.fi/onto/yso/p38633
jyx.subject.urihttp://www.yso.fi/onto/yso/p25709
jyx.subject.urihttp://www.yso.fi/onto/yso/p6486
jyx.subject.urihttp://www.yso.fi/onto/yso/p6956
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.3390/molecules25040879
dc.relation.funderSuomen Akatemiafi
dc.relation.funderAcademy of Finlanden
jyx.fundingprogramTutkijatohtori, SAfi
jyx.fundingprogramPostdoctoral Researcher, AoFen
jyx.fundinginformationThe authors thank Turku University Foundation for financial support. SS received financial support from the National Graduate School in Informational and Structural Biology, hosted by Åbo Akademi University, Finland. TAS and KMD acknowledge the Biocenter Finland technology platforms of bioinformatics (J.V. Lehtonen), translational activities and structural biology (Instruct-FI) at the Structural Bioinformatics Laboratory. TAS and KMD also thank the CSC IT Center for Science for laboratory and computational infrastructure support. This work was supported by the Sigrid Juselius Foundation (TAS, KMD) and Tor, Joe, and Pentti Borg’s Foundation (TAS). The authors gratefully acknowledge financial support from the Academy of Finland (RP: grant no. 298817) and the University of Jyväskylä.


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