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Synthesis 2017; 49(21): 4853-4860
DOI: 10.1055/s-0036-1590804
paper
© Georg Thieme Verlag Stuttgart · New York

The Chemoenzymatic Synthesis of 2-Chloro- and 2-Fluorocordycepins

Alexandra O. Denisova
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Yulia A. Tokunova
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Ilja V. Fateev
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Alexandra A. Breslav
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Vladimir N. Leonov
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Elena V. Dorofeeva
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Olga I. Lutonina
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Inessa S. Muzyka
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Roman S. Esipov
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Alexey L. Kayushin
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Irina D. Konstantinova
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Anatoly I. Miroshnikov
a   Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow B-437, 117997 GSP-7, Russian Federation
,
Vladimir A. Stepchenko
b   Institute of Bioorganic Chemistry, National Academy of Sciences, Acad. Kuprevicha 5/2, 220141 Minsk, Belarus   eMail: imikhailopulo@gmail.com
,
Igor A. Mikhailopulo*
b   Institute of Bioorganic Chemistry, National Academy of Sciences, Acad. Kuprevicha 5/2, 220141 Minsk, Belarus   eMail: imikhailopulo@gmail.com
› InstitutsangabenFinancial support by the International Science and Technology Centre (project #B-1640) and the Byelorussian Republican Foundation for Fundamental Research (project No. X13MC-027) is gratefully acknowledged.
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Publikationsverlauf

Received: 04. April 2017

Accepted after revision: 25. Mai 2017

Publikationsdatum:
20. Juli 2017 (online)

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Abstract

Two approaches to the chemoenzymatic synthesis of 2-fluorocordycepin and 2-chlorocordycepin were studied: (i) the use of 3′-deoxyadenosine (cordycepin) and 3′-deoxyinosine (3′dIno) as donors of 3-deoxy-d-ribofuranose in the transglycosylation of 2-fluoro- (2FAde) and 2-chloroadenine (2ClAde) catalyzed by the recombinant E. coli purine nucleoside phosphorylase (PNP), and (ii) the use of 2-fluoroadenosine and 3′-deoxyinosine as substrates of the cross-glycosylation and PNP as a biocatalyst. An efficient method for 3′-deoxyinosine synthesis starting from inosine was developed. However, the very poor solubility of 2ClAde and 2FAde is the limiting factor of the first approach. The second approach enables this problem to be overcome and it appears to be advantageous over the former approach from the viewpoint of practical synthesis of the title nucleosides. The 3-deoxy-α-d-ribofuranose-1-phosphate intermediary formed in the 3′dIno phosphorolysis by PNP was found to be the weak and marginal substrate of E. coli thymidine (TP) and uridine (UP) phosphorylases, respectively. Finally, one-pot cascade transformation of 3-deoxy-d-ribose in cordycepin in the presence of adenine and E. coli ribokinase, phosphopentomutase, and PNP was tested and cordycepin formation in ca. 3.4% yield was proved.

Key words

2-chlorocordycepin - 2-fluorocordycepin - 3′-deoxyinosine - 2-fluoroadenosine - E. coli nucleoside phosphorylases

Supporting Information

    Supporting information for this article is available online at https://doi.org/10.1055/s-0036-1590804.
  • Supporting Information
 

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