Version 1
: Received: 14 June 2024 / Approved: 14 June 2024 / Online: 14 June 2024 (15:24:21 CEST)
How to cite:
Cristofori, V.; Illuminati, D.; Bisquoli, C.; Catani, M.; Compagnin, G.; Turrin, G.; Trapella, C.; Fantinati, A. Enzymatic Desymmetrisation of Prochiral Meso-1,2-Disubstituted-1,2-Diaminoethane for the Synthesis of Key Enantioenriched (-)-Nutlin-3 Precursor. Preprints2024, 2024061026. https://doi.org/10.20944/preprints202406.1026.v1
Cristofori, V.; Illuminati, D.; Bisquoli, C.; Catani, M.; Compagnin, G.; Turrin, G.; Trapella, C.; Fantinati, A. Enzymatic Desymmetrisation of Prochiral Meso-1,2-Disubstituted-1,2-Diaminoethane for the Synthesis of Key Enantioenriched (-)-Nutlin-3 Precursor. Preprints 2024, 2024061026. https://doi.org/10.20944/preprints202406.1026.v1
Cristofori, V.; Illuminati, D.; Bisquoli, C.; Catani, M.; Compagnin, G.; Turrin, G.; Trapella, C.; Fantinati, A. Enzymatic Desymmetrisation of Prochiral Meso-1,2-Disubstituted-1,2-Diaminoethane for the Synthesis of Key Enantioenriched (-)-Nutlin-3 Precursor. Preprints2024, 2024061026. https://doi.org/10.20944/preprints202406.1026.v1
APA Style
Cristofori, V., Illuminati, D., Bisquoli, C., Catani, M., Compagnin, G., Turrin, G., Trapella, C., & Fantinati, A. (2024). Enzymatic Desymmetrisation of Prochiral Meso-1,2-Disubstituted-1,2-Diaminoethane for the Synthesis of Key Enantioenriched (-)-Nutlin-3 Precursor. Preprints. https://doi.org/10.20944/preprints202406.1026.v1
Chicago/Turabian Style
Cristofori, V., Claudio Trapella and Anna Fantinati. 2024 "Enzymatic Desymmetrisation of Prochiral Meso-1,2-Disubstituted-1,2-Diaminoethane for the Synthesis of Key Enantioenriched (-)-Nutlin-3 Precursor" Preprints. https://doi.org/10.20944/preprints202406.1026.v1
Abstract
Herein we present the biocatalysed preparation of mono-N-carbamate-protected precursor of antitumoral Nutlin-3a, through enantioselective alkoxycarbonylation of meso-1,2-disubstituted-1,2-diaminoethane, using enzyme lipases and dialkyl carbonates as acylating agents. A series of supported or free lipase enzymes were screened in combination with commercially available diallyl-, diethyl and dimethyl- carbonate. The reactions were conducted at different temperatures, reaction times and with variable co-solvent systems to evaluate the effect on the enzyme catalytic activity. The best results in terms of conversion, enantiomeric excess and yield were obtained when lipase from Candida antarctica B (CAL-B) was used with diallyl carbonate (DAC) conducting the reaction solventless at 75 °C.
Chemistry and Materials Science, Organic Chemistry
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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