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...
Published in: | Molecules |
---|---|
Main Authors: | , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
MDPI
2020
|
Subjects: | |
Online Access: | http://urn.fi/URN:NBN:fi:jyu-202002282224 |
id |
ftjyvaeskylaenun:oai:jyx.jyu.fi:123456789/68001 |
---|---|
record_format |
openpolar |
spelling |
ftjyvaeskylaenun:oai:jyx.jyu.fi:123456789/68001 2024-05-19T07:32:06+00:00 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 application/pdf fulltext http://urn.fi/URN:NBN:fi:jyu-202002282224 eng eng MDPI Molecules 1420-3049 4 25 298817 10.3390/molecules25040879 Research Council of Finland Suomen Akatemia Sirén, 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. Molecules , 25 (4), Article 879. https://doi.org/10.3390/molecules25040879 CONVID_34751885 URN:NBN:fi:jyu-202002282224 http://urn.fi/URN:NBN:fi:jyu-202002282224 CC BY 4.0 © 2020 by the authors. Licensee MDPI, Basel, Switzerland. openAccess https://creativecommons.org/licenses/by/4.0/ biocatalysis lipase A from Candida antarctica DIBO kinetic resolution molecular modeling entsyymit aromaattiset yhdisteet merkkiaineet laskennallinen kemia biokatalyysi lipaasit hiivasienet luonnonaineet article http://purl.org/eprint/type/JournalArticle http://purl.org/coar/resource_type/c_2df8fbb1 publishedVersion A1 2020 ftjyvaeskylaenun 2024-04-23T23:38:28Z 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; 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. peerReviewed Article in Journal/Newspaper Antarc* Antarctica JYX - Jyväskylä University Digital Archive Molecules 25 4 879 |
institution |
Open Polar |
collection |
JYX - Jyväskylä University Digital Archive |
op_collection_id |
ftjyvaeskylaenun |
language |
English |
topic |
biocatalysis lipase A from Candida antarctica DIBO kinetic resolution molecular modeling entsyymit aromaattiset yhdisteet merkkiaineet laskennallinen kemia biokatalyysi lipaasit hiivasienet luonnonaineet |
spellingShingle |
biocatalysis lipase A from Candida antarctica DIBO kinetic resolution molecular modeling entsyymit aromaattiset yhdisteet merkkiaineet laskennallinen kemia biokatalyysi lipaasit hiivasienet luonnonaineet 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 |
topic_facet |
biocatalysis lipase A from Candida antarctica DIBO kinetic resolution molecular modeling entsyymit aromaattiset yhdisteet merkkiaineet laskennallinen kemia biokatalyysi lipaasit hiivasienet luonnonaineet |
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 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. peerReviewed |
format |
Article in Journal/Newspaper |
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://urn.fi/URN:NBN:fi:jyu-202002282224 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
Molecules 1420-3049 4 25 298817 10.3390/molecules25040879 Research Council of Finland Suomen Akatemia Sirén, 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. Molecules , 25 (4), Article 879. https://doi.org/10.3390/molecules25040879 CONVID_34751885 URN:NBN:fi:jyu-202002282224 http://urn.fi/URN:NBN:fi:jyu-202002282224 |
op_rights |
CC BY 4.0 © 2020 by the authors. Licensee MDPI, Basel, Switzerland. openAccess https://creativecommons.org/licenses/by/4.0/ |
container_title |
Molecules |
container_volume |
25 |
container_issue |
4 |
container_start_page |
879 |
_version_ |
1799470059752521728 |