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7-Acylamino-3H-1,2-benzoxathiepine 2,2-dioxides as new isoform-selective carbonic anhydrase IX and XII inhibitors. / Pustenko, Aleksandrs; Nocentini, Alessio; Balašova, Anastasija; Krasavin, Mikhail; Žalubovskis, Raivis; Supuran, Claudiu T.

в: Journal of Enzyme Inhibition and Medicinal Chemistry, Том 35, № 1, 01.12.2020, стр. 650-656.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Pustenko, A, Nocentini, A, Balašova, A, Krasavin, M, Žalubovskis, R & Supuran, CT 2020, '7-Acylamino-3H-1,2-benzoxathiepine 2,2-dioxides as new isoform-selective carbonic anhydrase IX and XII inhibitors', Journal of Enzyme Inhibition and Medicinal Chemistry, Том. 35, № 1, стр. 650-656. https://doi.org/10.1080/14756366.2020.1722658

APA

Pustenko, A., Nocentini, A., Balašova, A., Krasavin, M., Žalubovskis, R., & Supuran, C. T. (2020). 7-Acylamino-3H-1,2-benzoxathiepine 2,2-dioxides as new isoform-selective carbonic anhydrase IX and XII inhibitors. Journal of Enzyme Inhibition and Medicinal Chemistry, 35(1), 650-656. https://doi.org/10.1080/14756366.2020.1722658

Vancouver

Pustenko A, Nocentini A, Balašova A, Krasavin M, Žalubovskis R, Supuran CT. 7-Acylamino-3H-1,2-benzoxathiepine 2,2-dioxides as new isoform-selective carbonic anhydrase IX and XII inhibitors. Journal of Enzyme Inhibition and Medicinal Chemistry. 2020 Дек. 1;35(1):650-656. https://doi.org/10.1080/14756366.2020.1722658

Author

Pustenko, Aleksandrs ; Nocentini, Alessio ; Balašova, Anastasija ; Krasavin, Mikhail ; Žalubovskis, Raivis ; Supuran, Claudiu T. / 7-Acylamino-3H-1,2-benzoxathiepine 2,2-dioxides as new isoform-selective carbonic anhydrase IX and XII inhibitors. в: Journal of Enzyme Inhibition and Medicinal Chemistry. 2020 ; Том 35, № 1. стр. 650-656.

BibTeX

@article{726a0f8748634f0389a265103473cb3e,
title = "7-Acylamino-3H-1,2-benzoxathiepine 2,2-dioxides as new isoform-selective carbonic anhydrase IX and XII inhibitors",
abstract = "A series of 3H-1,2-benzoxathiepine 2,2-dioxides incorporating 7-acylamino moieties were obtained by an original procedure starting from 5-nitrosalicylaldehyde, which was treated with propenylsulfonyl chloride followed by Wittig reaction of the bis-olefin intermediate. The new derivatives, belonging to the homosulfocoumarin chemotype, were assayed as inhibitors of the zinc metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1). Four pharmacologically relevant human (h) isoforms were investigated, the cytosolic hCA I and II and the transmembrane, tumour-associated hCA IX and XII. No relevant inhibition of hCA I and II was observed, whereas some of the new derivatives were effective, low nanomolar hCA IX/XII inhibitors, making them of interest for investigations in situations in which the activity of these isoforms is overexpressed, such as hypoxic tumours, arthritis or cerebral ischaemia.",
keywords = "Carbonic anhydrase, homosulfocoumarin, isoform-selective inhibitor, sulfocoumarin, transmembrane isoforms, TRANSMEMBRANE, SULFONAMIDES, ALPHA, ISOZYMES I, BACTERIAL, COUMARINS, DISCOVERY, POTENT, SULFOCOUMARINS, DERIVATIVES",
author = "Aleksandrs Pustenko and Alessio Nocentini and Anastasija Bala{\v s}ova and Mikhail Krasavin and Raivis {\v Z}alubovskis and Supuran, {Claudiu T.}",
note = "Funding Information: This work was partly supported by ERA.Net RUS plus joint programme project THIOREDIN (State Education Development Agency of Republic of Latvia) and the Russian Foundation for Basic Research [project grant 18?515-76001] under ERA.Net RUS plus joint programme grant RUS_ST2017-309. Publisher Copyright: {\textcopyright} 2020, {\textcopyright} 2020 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.",
year = "2020",
month = dec,
day = "1",
doi = "10.1080/14756366.2020.1722658",
language = "Английский",
volume = "35",
pages = "650--656",
journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
issn = "1475-6366",
publisher = "Taylor & Francis",
number = "1",

}

RIS

TY - JOUR

T1 - 7-Acylamino-3H-1,2-benzoxathiepine 2,2-dioxides as new isoform-selective carbonic anhydrase IX and XII inhibitors

AU - Pustenko, Aleksandrs

AU - Nocentini, Alessio

AU - Balašova, Anastasija

AU - Krasavin, Mikhail

AU - Žalubovskis, Raivis

AU - Supuran, Claudiu T.

N1 - Funding Information: This work was partly supported by ERA.Net RUS plus joint programme project THIOREDIN (State Education Development Agency of Republic of Latvia) and the Russian Foundation for Basic Research [project grant 18?515-76001] under ERA.Net RUS plus joint programme grant RUS_ST2017-309. Publisher Copyright: © 2020, © 2020 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

PY - 2020/12/1

Y1 - 2020/12/1

N2 - A series of 3H-1,2-benzoxathiepine 2,2-dioxides incorporating 7-acylamino moieties were obtained by an original procedure starting from 5-nitrosalicylaldehyde, which was treated with propenylsulfonyl chloride followed by Wittig reaction of the bis-olefin intermediate. The new derivatives, belonging to the homosulfocoumarin chemotype, were assayed as inhibitors of the zinc metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1). Four pharmacologically relevant human (h) isoforms were investigated, the cytosolic hCA I and II and the transmembrane, tumour-associated hCA IX and XII. No relevant inhibition of hCA I and II was observed, whereas some of the new derivatives were effective, low nanomolar hCA IX/XII inhibitors, making them of interest for investigations in situations in which the activity of these isoforms is overexpressed, such as hypoxic tumours, arthritis or cerebral ischaemia.

AB - A series of 3H-1,2-benzoxathiepine 2,2-dioxides incorporating 7-acylamino moieties were obtained by an original procedure starting from 5-nitrosalicylaldehyde, which was treated with propenylsulfonyl chloride followed by Wittig reaction of the bis-olefin intermediate. The new derivatives, belonging to the homosulfocoumarin chemotype, were assayed as inhibitors of the zinc metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1). Four pharmacologically relevant human (h) isoforms were investigated, the cytosolic hCA I and II and the transmembrane, tumour-associated hCA IX and XII. No relevant inhibition of hCA I and II was observed, whereas some of the new derivatives were effective, low nanomolar hCA IX/XII inhibitors, making them of interest for investigations in situations in which the activity of these isoforms is overexpressed, such as hypoxic tumours, arthritis or cerebral ischaemia.

KW - Carbonic anhydrase

KW - homosulfocoumarin

KW - isoform-selective inhibitor

KW - sulfocoumarin

KW - transmembrane isoforms

KW - TRANSMEMBRANE

KW - SULFONAMIDES

KW - ALPHA

KW - ISOZYMES I

KW - BACTERIAL

KW - COUMARINS

KW - DISCOVERY

KW - POTENT

KW - SULFOCOUMARINS

KW - DERIVATIVES

UR - http://www.scopus.com/inward/record.url?scp=85079752261&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/43a37b69-0a2f-3bf9-b7a5-5e7f7e86db11/

U2 - 10.1080/14756366.2020.1722658

DO - 10.1080/14756366.2020.1722658

M3 - статья

C2 - 32079427

AN - SCOPUS:85079752261

VL - 35

SP - 650

EP - 656

JO - Journal of Enzyme Inhibition and Medicinal Chemistry

JF - Journal of Enzyme Inhibition and Medicinal Chemistry

SN - 1475-6366

IS - 1

ER -

ID: 52203682