Design, synthesis and α-glucosidase inhibition study of novel pyridazin-based derivatives
In this paper, pyridazin derivatives containing different thiobenzyl moieties were synthesized and screened for their inhibitory activities against rat intestinal α-glucosidase enzyme. The final products were easily obtained without the need to harsh purification steps. The in vitro results revealed...
Gespeichert in:
| Veröffentlicht in: | Medicinal chemistry research 2023-04, Vol.32 (4), p.713-722 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 722 |
|---|---|
| container_issue | 4 |
| container_start_page | 713 |
| container_title | Medicinal chemistry research |
| container_volume | 32 |
| creator | Firoozpour, Loghman Kazemzadeh Arasi, Faraz Toolabi, Mahsa Moghimi, Setareh Armandeh, Maryam Salmani, Farzaneh Pakrad, Roya Firuzpour, Hadis Ghasemi Dogaheh, Mahtab Ebrahimi, Seyed Esmaeil Sadat H.M.E. Ketabforoosh, Shima Karima, Saeed Foroumadi, Alireza |
| description | In this paper, pyridazin derivatives containing different thiobenzyl moieties were synthesized and screened for their inhibitory activities against rat intestinal α-glucosidase enzyme. The final products were easily obtained without the need to harsh purification steps. The in vitro results revealed that all the synthesized compounds were more potent (IC
50
s = 26.3–148.9 μM) than the clinically used drug, acarbose. The kinetic study revealed the competitive inhibition behavior of compound
5m
(K
i
= −56 μM). Docking studies showed imperative interactions such as hydrogen bonding, Pi-Pi T-shaped, and Pi-anion interactions confirming the observed activity. The RMSD value was determined less than 3 Å and validated the study.
Graphical Abstract |
| doi_str_mv | 10.1007/s00044-023-03027-9 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_2783898341</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2783898341</sourcerecordid><originalsourceid>FETCH-LOGICAL-c319t-598f4b29d5dbfc2660f0a35af77b6695690fc9deca57bb1a6a021759708717393</originalsourceid><addsrcrecordid>eNp9kL1OwzAUhS0EEuXnBZgssWK4tuM4HlH5lSqxwMJiOYnduipOsZNK5a14EZ4JlyCxMd0zfOdc6UPojMIlBZBXCQCKggDjBDgwSdQemlAhClJRBvs5Q85MMH6IjlJaAnAJhZig1xub_Dxc4LQN_SLnhE1o8dcnma-Gpku-NcliHxa-9r3vAk790G5x53DoNnaF19uYkQ8fSJ3BFrc2-o3p_camE3TgzCrZ0997jF7ubp-nD2T2dP84vZ6RhlPVE6EqV9RMtaKtXcPKEhwYLoyTsi5LJUoFrlGtbYyQdU1NaYBRKZSESlLJFT9G5-PuOnbvg029XnZDDPmlZrLilap4QTPFRqqJXUrROr2O_s3Eraagdw716FBnh_rHod5N87GUMhzmNv5N_9P6BriIdZg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2783898341</pqid></control><display><type>article</type><title>Design, synthesis and α-glucosidase inhibition study of novel pyridazin-based derivatives</title><source>SpringerLink Journals</source><creator>Firoozpour, Loghman ; Kazemzadeh Arasi, Faraz ; Toolabi, Mahsa ; Moghimi, Setareh ; Armandeh, Maryam ; Salmani, Farzaneh ; Pakrad, Roya ; Firuzpour, Hadis ; Ghasemi Dogaheh, Mahtab ; Ebrahimi, Seyed Esmaeil Sadat ; H.M.E. Ketabforoosh, Shima ; Karima, Saeed ; Foroumadi, Alireza</creator><creatorcontrib>Firoozpour, Loghman ; Kazemzadeh Arasi, Faraz ; Toolabi, Mahsa ; Moghimi, Setareh ; Armandeh, Maryam ; Salmani, Farzaneh ; Pakrad, Roya ; Firuzpour, Hadis ; Ghasemi Dogaheh, Mahtab ; Ebrahimi, Seyed Esmaeil Sadat ; H.M.E. Ketabforoosh, Shima ; Karima, Saeed ; Foroumadi, Alireza</creatorcontrib><description>In this paper, pyridazin derivatives containing different thiobenzyl moieties were synthesized and screened for their inhibitory activities against rat intestinal α-glucosidase enzyme. The final products were easily obtained without the need to harsh purification steps. The in vitro results revealed that all the synthesized compounds were more potent (IC
50
s = 26.3–148.9 μM) than the clinically used drug, acarbose. The kinetic study revealed the competitive inhibition behavior of compound
5m
(K
i
= −56 μM). Docking studies showed imperative interactions such as hydrogen bonding, Pi-Pi T-shaped, and Pi-anion interactions confirming the observed activity. The RMSD value was determined less than 3 Å and validated the study.
Graphical Abstract</description><identifier>ISSN: 1054-2523</identifier><identifier>EISSN: 1554-8120</identifier><identifier>DOI: 10.1007/s00044-023-03027-9</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Acarbose ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Bioorganic Chemistry ; Glucosidase ; Hydrogen bonding ; Inorganic Chemistry ; Medicinal Chemistry ; Original Research ; Pharmacology/Toxicology ; Synthesis ; α-Glucosidase</subject><ispartof>Medicinal chemistry research, 2023-04, Vol.32 (4), p.713-722</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c319t-598f4b29d5dbfc2660f0a35af77b6695690fc9deca57bb1a6a021759708717393</citedby><cites>FETCH-LOGICAL-c319t-598f4b29d5dbfc2660f0a35af77b6695690fc9deca57bb1a6a021759708717393</cites><orcidid>0000-0003-2416-5611</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00044-023-03027-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00044-023-03027-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Firoozpour, Loghman</creatorcontrib><creatorcontrib>Kazemzadeh Arasi, Faraz</creatorcontrib><creatorcontrib>Toolabi, Mahsa</creatorcontrib><creatorcontrib>Moghimi, Setareh</creatorcontrib><creatorcontrib>Armandeh, Maryam</creatorcontrib><creatorcontrib>Salmani, Farzaneh</creatorcontrib><creatorcontrib>Pakrad, Roya</creatorcontrib><creatorcontrib>Firuzpour, Hadis</creatorcontrib><creatorcontrib>Ghasemi Dogaheh, Mahtab</creatorcontrib><creatorcontrib>Ebrahimi, Seyed Esmaeil Sadat</creatorcontrib><creatorcontrib>H.M.E. Ketabforoosh, Shima</creatorcontrib><creatorcontrib>Karima, Saeed</creatorcontrib><creatorcontrib>Foroumadi, Alireza</creatorcontrib><title>Design, synthesis and α-glucosidase inhibition study of novel pyridazin-based derivatives</title><title>Medicinal chemistry research</title><addtitle>Med Chem Res</addtitle><description>In this paper, pyridazin derivatives containing different thiobenzyl moieties were synthesized and screened for their inhibitory activities against rat intestinal α-glucosidase enzyme. The final products were easily obtained without the need to harsh purification steps. The in vitro results revealed that all the synthesized compounds were more potent (IC
50
s = 26.3–148.9 μM) than the clinically used drug, acarbose. The kinetic study revealed the competitive inhibition behavior of compound
5m
(K
i
= −56 μM). Docking studies showed imperative interactions such as hydrogen bonding, Pi-Pi T-shaped, and Pi-anion interactions confirming the observed activity. The RMSD value was determined less than 3 Å and validated the study.
Graphical Abstract</description><subject>Acarbose</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bioorganic Chemistry</subject><subject>Glucosidase</subject><subject>Hydrogen bonding</subject><subject>Inorganic Chemistry</subject><subject>Medicinal Chemistry</subject><subject>Original Research</subject><subject>Pharmacology/Toxicology</subject><subject>Synthesis</subject><subject>α-Glucosidase</subject><issn>1054-2523</issn><issn>1554-8120</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNp9kL1OwzAUhS0EEuXnBZgssWK4tuM4HlH5lSqxwMJiOYnduipOsZNK5a14EZ4JlyCxMd0zfOdc6UPojMIlBZBXCQCKggDjBDgwSdQemlAhClJRBvs5Q85MMH6IjlJaAnAJhZig1xub_Dxc4LQN_SLnhE1o8dcnma-Gpku-NcliHxa-9r3vAk790G5x53DoNnaF19uYkQ8fSJ3BFrc2-o3p_camE3TgzCrZ0997jF7ubp-nD2T2dP84vZ6RhlPVE6EqV9RMtaKtXcPKEhwYLoyTsi5LJUoFrlGtbYyQdU1NaYBRKZSESlLJFT9G5-PuOnbvg029XnZDDPmlZrLilap4QTPFRqqJXUrROr2O_s3Eraagdw716FBnh_rHod5N87GUMhzmNv5N_9P6BriIdZg</recordid><startdate>20230401</startdate><enddate>20230401</enddate><creator>Firoozpour, Loghman</creator><creator>Kazemzadeh Arasi, Faraz</creator><creator>Toolabi, Mahsa</creator><creator>Moghimi, Setareh</creator><creator>Armandeh, Maryam</creator><creator>Salmani, Farzaneh</creator><creator>Pakrad, Roya</creator><creator>Firuzpour, Hadis</creator><creator>Ghasemi Dogaheh, Mahtab</creator><creator>Ebrahimi, Seyed Esmaeil Sadat</creator><creator>H.M.E. Ketabforoosh, Shima</creator><creator>Karima, Saeed</creator><creator>Foroumadi, Alireza</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><orcidid>https://orcid.org/0000-0003-2416-5611</orcidid></search><sort><creationdate>20230401</creationdate><title>Design, synthesis and α-glucosidase inhibition study of novel pyridazin-based derivatives</title><author>Firoozpour, Loghman ; Kazemzadeh Arasi, Faraz ; Toolabi, Mahsa ; Moghimi, Setareh ; Armandeh, Maryam ; Salmani, Farzaneh ; Pakrad, Roya ; Firuzpour, Hadis ; Ghasemi Dogaheh, Mahtab ; Ebrahimi, Seyed Esmaeil Sadat ; H.M.E. Ketabforoosh, Shima ; Karima, Saeed ; Foroumadi, Alireza</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c319t-598f4b29d5dbfc2660f0a35af77b6695690fc9deca57bb1a6a021759708717393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Acarbose</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Bioorganic Chemistry</topic><topic>Glucosidase</topic><topic>Hydrogen bonding</topic><topic>Inorganic Chemistry</topic><topic>Medicinal Chemistry</topic><topic>Original Research</topic><topic>Pharmacology/Toxicology</topic><topic>Synthesis</topic><topic>α-Glucosidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Firoozpour, Loghman</creatorcontrib><creatorcontrib>Kazemzadeh Arasi, Faraz</creatorcontrib><creatorcontrib>Toolabi, Mahsa</creatorcontrib><creatorcontrib>Moghimi, Setareh</creatorcontrib><creatorcontrib>Armandeh, Maryam</creatorcontrib><creatorcontrib>Salmani, Farzaneh</creatorcontrib><creatorcontrib>Pakrad, Roya</creatorcontrib><creatorcontrib>Firuzpour, Hadis</creatorcontrib><creatorcontrib>Ghasemi Dogaheh, Mahtab</creatorcontrib><creatorcontrib>Ebrahimi, Seyed Esmaeil Sadat</creatorcontrib><creatorcontrib>H.M.E. Ketabforoosh, Shima</creatorcontrib><creatorcontrib>Karima, Saeed</creatorcontrib><creatorcontrib>Foroumadi, Alireza</creatorcontrib><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Medicinal chemistry research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Firoozpour, Loghman</au><au>Kazemzadeh Arasi, Faraz</au><au>Toolabi, Mahsa</au><au>Moghimi, Setareh</au><au>Armandeh, Maryam</au><au>Salmani, Farzaneh</au><au>Pakrad, Roya</au><au>Firuzpour, Hadis</au><au>Ghasemi Dogaheh, Mahtab</au><au>Ebrahimi, Seyed Esmaeil Sadat</au><au>H.M.E. Ketabforoosh, Shima</au><au>Karima, Saeed</au><au>Foroumadi, Alireza</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Design, synthesis and α-glucosidase inhibition study of novel pyridazin-based derivatives</atitle><jtitle>Medicinal chemistry research</jtitle><stitle>Med Chem Res</stitle><date>2023-04-01</date><risdate>2023</risdate><volume>32</volume><issue>4</issue><spage>713</spage><epage>722</epage><pages>713-722</pages><issn>1054-2523</issn><eissn>1554-8120</eissn><abstract>In this paper, pyridazin derivatives containing different thiobenzyl moieties were synthesized and screened for their inhibitory activities against rat intestinal α-glucosidase enzyme. The final products were easily obtained without the need to harsh purification steps. The in vitro results revealed that all the synthesized compounds were more potent (IC
50
s = 26.3–148.9 μM) than the clinically used drug, acarbose. The kinetic study revealed the competitive inhibition behavior of compound
5m
(K
i
= −56 μM). Docking studies showed imperative interactions such as hydrogen bonding, Pi-Pi T-shaped, and Pi-anion interactions confirming the observed activity. The RMSD value was determined less than 3 Å and validated the study.
Graphical Abstract</abstract><cop>New York</cop><pub>Springer US</pub><doi>10.1007/s00044-023-03027-9</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-2416-5611</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1054-2523 |
| ispartof | Medicinal chemistry research, 2023-04, Vol.32 (4), p.713-722 |
| issn | 1054-2523 1554-8120 |
| language | eng |
| recordid | cdi_proquest_journals_2783898341 |
| source | SpringerLink Journals |
| subjects | Acarbose Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Glucosidase Hydrogen bonding Inorganic Chemistry Medicinal Chemistry Original Research Pharmacology/Toxicology Synthesis α-Glucosidase |
| title | Design, synthesis and α-glucosidase inhibition study of novel pyridazin-based derivatives |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-27T07%3A11%3A42IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Design,%20synthesis%20and%20%CE%B1-glucosidase%20inhibition%20study%20of%20novel%20pyridazin-based%20derivatives&rft.jtitle=Medicinal%20chemistry%20research&rft.au=Firoozpour,%20Loghman&rft.date=2023-04-01&rft.volume=32&rft.issue=4&rft.spage=713&rft.epage=722&rft.pages=713-722&rft.issn=1054-2523&rft.eissn=1554-8120&rft_id=info:doi/10.1007/s00044-023-03027-9&rft_dat=%3Cproquest_cross%3E2783898341%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2783898341&rft_id=info:pmid/&rfr_iscdi=true |