Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging
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)-D...
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ftpubmed:oai:pubmedcentral.nih.gov:7070869 2023-05-15T14:03:03+02:00 Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging Sirén, Saija Dahlström, Käthe M. Puttreddy, Rakesh Rissanen, Kari Salminen, Tiina A. Scheinin, Mika Li, Xiang-Guo Liljeblad, Arto 2020-02-17 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7070869/ http://www.ncbi.nlm.nih.gov/pubmed/32079253 https://doi.org/10.3390/molecules25040879 en eng MDPI http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7070869/ http://www.ncbi.nlm.nih.gov/pubmed/32079253 http://dx.doi.org/10.3390/molecules25040879 © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). CC-BY Article Text 2020 ftpubmed https://doi.org/10.3390/molecules25040879 2020-03-22T01:43:47Z 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 MgCl(2) 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 MgCl(2)·6H(2)O also allowed high conversion or effect on enantioselectivity, Mg(2+) 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. Text Antarc* Antarctica PubMed Central (PMC) Molecules 25 4 879 |
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Article Sirén, Saija Dahlström, Käthe M. Puttreddy, Rakesh Rissanen, Kari Salminen, Tiina A. Scheinin, Mika Li, Xiang-Guo Liljeblad, Arto Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging |
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Article |
description |
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 MgCl(2) 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 MgCl(2)·6H(2)O also allowed high conversion or effect on enantioselectivity, Mg(2+) 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. |
format |
Text |
author |
Sirén, Saija Dahlström, Käthe M. Puttreddy, Rakesh Rissanen, Kari Salminen, Tiina A. Scheinin, Mika Li, Xiang-Guo Liljeblad, Arto |
author_facet |
Sirén, Saija Dahlström, Käthe M. Puttreddy, Rakesh Rissanen, Kari Salminen, Tiina A. Scheinin, Mika Li, Xiang-Guo Liljeblad, Arto |
author_sort |
Sirén, Saija |
title |
Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging |
title_short |
Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging |
title_full |
Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging |
title_fullStr |
Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging |
title_full_unstemmed |
Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging |
title_sort |
candida antarctica lipase a-based enantiorecognition of a highly strained 4-dibenzocyclooctynol (dibo) used for pet imaging |
publisher |
MDPI |
publishDate |
2020 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7070869/ http://www.ncbi.nlm.nih.gov/pubmed/32079253 https://doi.org/10.3390/molecules25040879 |
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Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7070869/ http://www.ncbi.nlm.nih.gov/pubmed/32079253 http://dx.doi.org/10.3390/molecules25040879 |
op_rights |
© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
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CC-BY |
op_doi |
https://doi.org/10.3390/molecules25040879 |
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Molecules |
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