Synthetic heterocyclic candidates as promising α-glucosidase inhibitors: An overview
α-Glucosidase enzyme inhibition is an effective therapeutic decorum in the treatment of type 2 diabetes mellitus. Since 1990, three α-glucosidase inhibitors are known to exist clinically, Acarbose, Voglibose and Miglitol. Side effects and long synthetic routes to access them forced the researchers t...
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| Veröffentlicht in: | European journal of medicinal chemistry 2019-08, Vol.176, p.343-377 |
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| container_title | European journal of medicinal chemistry |
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| creator | Dhameja, Manoj Gupta, Preeti |
| description | α-Glucosidase enzyme inhibition is an effective therapeutic decorum in the treatment of type 2 diabetes mellitus. Since 1990, three α-glucosidase inhibitors are known to exist clinically, Acarbose, Voglibose and Miglitol. Side effects and long synthetic routes to access them forced the researchers to move their focus to discover simple and small heterocyclic motifs that work as promising α-glucosidase inhibitors and may eventually lead to the management of postprandial hyperglycemic condition in T2DM. In this regards, this review deals with recently discovered heterocyclic molecules that have been evaluated to exhibit inhibition of α-glucosidase enzyme.
[Display omitted]
•Recently designed and developed heterocyclic α-glucosidase inhibitors.•All synthetic heterocyclic derivatives and hybrids covered till 2018 literature.•Structural activity relationship (SAR) of heterocyclic α-glucosidase inhibitors included.•Binding interactions of most active inhibitors discussed. |
| doi_str_mv | 10.1016/j.ejmech.2019.04.025 |
| format | Article |
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[Display omitted]
•Recently designed and developed heterocyclic α-glucosidase inhibitors.•All synthetic heterocyclic derivatives and hybrids covered till 2018 literature.•Structural activity relationship (SAR) of heterocyclic α-glucosidase inhibitors included.•Binding interactions of most active inhibitors discussed.</description><identifier>ISSN: 0223-5234</identifier><identifier>EISSN: 1768-3254</identifier><identifier>DOI: 10.1016/j.ejmech.2019.04.025</identifier><identifier>PMID: 31112894</identifier><language>eng</language><publisher>France: Elsevier Masson SAS</publisher><subject>alpha-Glucosidases - chemistry ; alpha-Glucosidases - metabolism ; Animals ; Cell Line, Tumor ; Docking study ; Glycoside Hydrolase Inhibitors - chemistry ; Glycoside Hydrolase Inhibitors - metabolism ; Glycoside Hydrolase Inhibitors - pharmacology ; Glycoside Hydrolase Inhibitors - toxicity ; Heterocyclic compounds ; Heterocyclic Compounds - chemistry ; Heterocyclic Compounds - metabolism ; Heterocyclic Compounds - pharmacology ; Heterocyclic Compounds - toxicity ; Humans ; Hypoglycemic Agents - chemistry ; Hypoglycemic Agents - metabolism ; Hypoglycemic Agents - pharmacology ; Hypoglycemic Agents - toxicity ; Molecular Docking Simulation ; Molecular Structure ; Protein Binding ; Structure activity relationship (SAR) ; Structure-Activity Relationship ; α-Glucosidase inhibitors</subject><ispartof>European journal of medicinal chemistry, 2019-08, Vol.176, p.343-377</ispartof><rights>2019 Elsevier Masson SAS</rights><rights>Copyright © 2019 Elsevier Masson SAS. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c362t-5c168b52eaaf03231b75dcdaba083081ddc3485d5d67af43e174feaecc2348633</citedby><cites>FETCH-LOGICAL-c362t-5c168b52eaaf03231b75dcdaba083081ddc3485d5d67af43e174feaecc2348633</cites><orcidid>0000-0002-1679-0890 ; 0000-0002-7133-1873</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0223523419303319$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31112894$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dhameja, Manoj</creatorcontrib><creatorcontrib>Gupta, Preeti</creatorcontrib><title>Synthetic heterocyclic candidates as promising α-glucosidase inhibitors: An overview</title><title>European journal of medicinal chemistry</title><addtitle>Eur J Med Chem</addtitle><description>α-Glucosidase enzyme inhibition is an effective therapeutic decorum in the treatment of type 2 diabetes mellitus. Since 1990, three α-glucosidase inhibitors are known to exist clinically, Acarbose, Voglibose and Miglitol. Side effects and long synthetic routes to access them forced the researchers to move their focus to discover simple and small heterocyclic motifs that work as promising α-glucosidase inhibitors and may eventually lead to the management of postprandial hyperglycemic condition in T2DM. In this regards, this review deals with recently discovered heterocyclic molecules that have been evaluated to exhibit inhibition of α-glucosidase enzyme.
[Display omitted]
•Recently designed and developed heterocyclic α-glucosidase inhibitors.•All synthetic heterocyclic derivatives and hybrids covered till 2018 literature.•Structural activity relationship (SAR) of heterocyclic α-glucosidase inhibitors included.•Binding interactions of most active inhibitors discussed.</description><subject>alpha-Glucosidases - chemistry</subject><subject>alpha-Glucosidases - metabolism</subject><subject>Animals</subject><subject>Cell Line, Tumor</subject><subject>Docking study</subject><subject>Glycoside Hydrolase Inhibitors - chemistry</subject><subject>Glycoside Hydrolase Inhibitors - metabolism</subject><subject>Glycoside Hydrolase Inhibitors - pharmacology</subject><subject>Glycoside Hydrolase Inhibitors - toxicity</subject><subject>Heterocyclic compounds</subject><subject>Heterocyclic Compounds - chemistry</subject><subject>Heterocyclic Compounds - metabolism</subject><subject>Heterocyclic Compounds - pharmacology</subject><subject>Heterocyclic Compounds - toxicity</subject><subject>Humans</subject><subject>Hypoglycemic Agents - chemistry</subject><subject>Hypoglycemic Agents - metabolism</subject><subject>Hypoglycemic Agents - pharmacology</subject><subject>Hypoglycemic Agents - toxicity</subject><subject>Molecular Docking Simulation</subject><subject>Molecular Structure</subject><subject>Protein Binding</subject><subject>Structure activity relationship (SAR)</subject><subject>Structure-Activity Relationship</subject><subject>α-Glucosidase inhibitors</subject><issn>0223-5234</issn><issn>1768-3254</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtOwzAQhi0EoqVwA4SyZJPgZ5KyQEIVLwmJBbC2nPGEukqTYqdFPRYX4UwYpbBkM6PR_PP4P0JOGc0YZfnFIsPFEmGeccqmGZUZ5WqPjFmRl6ngSu6TMeVcpIoLOSJHISwopSqn9JCMBGOMl1M5Jq_P27afY-8giRF9B1toYgGmtc6aHkNiQrLy3dIF174lX5_pW7OGLsRmwMS1c1e5vvPhMrluk26DfuPw45gc1KYJeLLLE_J6e_Myu08fn-4eZtePKYic96kClpeV4mhMTQUXrCqUBWsqQ0tBS2YtCFkqq2xemFoKZIWs0SBA9FTmQkzI-bA3Pvi-xtDr-CZg05gWu3XQ0T8rVcHjugmRgxR8F4LHWq-8Wxq_1YzqH6B6oQeg-geoplJHoHHsbHdhXS3R_g39EoyCq0GA0Wf07nUAhy2gdR6h17Zz_1_4BoAFirw</recordid><startdate>20190815</startdate><enddate>20190815</enddate><creator>Dhameja, Manoj</creator><creator>Gupta, Preeti</creator><general>Elsevier Masson SAS</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-1679-0890</orcidid><orcidid>https://orcid.org/0000-0002-7133-1873</orcidid></search><sort><creationdate>20190815</creationdate><title>Synthetic heterocyclic candidates as promising α-glucosidase inhibitors: An overview</title><author>Dhameja, Manoj ; 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Since 1990, three α-glucosidase inhibitors are known to exist clinically, Acarbose, Voglibose and Miglitol. Side effects and long synthetic routes to access them forced the researchers to move their focus to discover simple and small heterocyclic motifs that work as promising α-glucosidase inhibitors and may eventually lead to the management of postprandial hyperglycemic condition in T2DM. In this regards, this review deals with recently discovered heterocyclic molecules that have been evaluated to exhibit inhibition of α-glucosidase enzyme.
[Display omitted]
•Recently designed and developed heterocyclic α-glucosidase inhibitors.•All synthetic heterocyclic derivatives and hybrids covered till 2018 literature.•Structural activity relationship (SAR) of heterocyclic α-glucosidase inhibitors included.•Binding interactions of most active inhibitors discussed.</abstract><cop>France</cop><pub>Elsevier Masson SAS</pub><pmid>31112894</pmid><doi>10.1016/j.ejmech.2019.04.025</doi><tpages>35</tpages><orcidid>https://orcid.org/0000-0002-1679-0890</orcidid><orcidid>https://orcid.org/0000-0002-7133-1873</orcidid></addata></record> |
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| ispartof | European journal of medicinal chemistry, 2019-08, Vol.176, p.343-377 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | alpha-Glucosidases - chemistry alpha-Glucosidases - metabolism Animals Cell Line, Tumor Docking study Glycoside Hydrolase Inhibitors - chemistry Glycoside Hydrolase Inhibitors - metabolism Glycoside Hydrolase Inhibitors - pharmacology Glycoside Hydrolase Inhibitors - toxicity Heterocyclic compounds Heterocyclic Compounds - chemistry Heterocyclic Compounds - metabolism Heterocyclic Compounds - pharmacology Heterocyclic Compounds - toxicity Humans Hypoglycemic Agents - chemistry Hypoglycemic Agents - metabolism Hypoglycemic Agents - pharmacology Hypoglycemic Agents - toxicity Molecular Docking Simulation Molecular Structure Protein Binding Structure activity relationship (SAR) Structure-Activity Relationship α-Glucosidase inhibitors |
| title | Synthetic heterocyclic candidates as promising α-glucosidase inhibitors: An overview |
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