Tetrahydroquinoline-Isoxazole/Isoxazoline Hybrid Compounds as Potential Cholinesterases Inhibitors: Synthesis, Enzyme Inhibition Assays, and Molecular Modeling Studies
A series of 44 hybrid compounds that included in their structure tetrahydroquinoline (THQ) and isoxazole/isoxazoline moieties were synthesized through the 1,3-dipolar cycloaddition reaction (1,3-DC) from the corresponding -allyl/propargyl THQs, previously obtained via cationic Povarov reaction. In v...
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| Veröffentlicht in: | International journal of molecular sciences 2019-12, Vol.21 (1), p.5 |
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| creator | Rodríguez Núñez, Yeray A Gutíerrez, Margarita Alzate-Morales, Jans Adasme-Carreño, Francisco Güiza, Fausto M Bernal, Cristian C Bohórquez, Arnold R Romero |
| description | A series of 44 hybrid compounds that included in their structure tetrahydroquinoline (THQ) and isoxazole/isoxazoline moieties were synthesized through the 1,3-dipolar cycloaddition reaction (1,3-DC) from the corresponding
-allyl/propargyl THQs, previously obtained via cationic Povarov reaction. In vitro cholinergic enzymes inhibition potential of all compounds was tested. Enzyme inhibition assays showed that some hybrids exhibited significant potency to inhibit acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Especially, the hybrid compound 5n presented the more effective inhibition against AChE (4.24 µM) with an acceptable selectivity index versus BChE (SI: 5.19), while compound 6aa exhibited the greatest inhibition activity on BChE (3.97 µM) and a significant selectivity index against AChE (SI: 0.04). Kinetic studies were carried out for compounds with greater inhibitory activity of cholinesterases. Structure-activity relationships of the molecular hybrids were analyzed, through computational models using a molecular cross-docking algorithm and Molecular Mechanics/Generalized Born Surface Area (MM/GBSA) binding free energy approach, which indicated a good correlation between the experimental inhibition values and the predicted free binding energy. |
| doi_str_mv | 10.3390/ijms21010005 |
| format | Article |
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-allyl/propargyl THQs, previously obtained via cationic Povarov reaction. In vitro cholinergic enzymes inhibition potential of all compounds was tested. Enzyme inhibition assays showed that some hybrids exhibited significant potency to inhibit acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Especially, the hybrid compound 5n presented the more effective inhibition against AChE (4.24 µM) with an acceptable selectivity index versus BChE (SI: 5.19), while compound 6aa exhibited the greatest inhibition activity on BChE (3.97 µM) and a significant selectivity index against AChE (SI: 0.04). Kinetic studies were carried out for compounds with greater inhibitory activity of cholinesterases. Structure-activity relationships of the molecular hybrids were analyzed, through computational models using a molecular cross-docking algorithm and Molecular Mechanics/Generalized Born Surface Area (MM/GBSA) binding free energy approach, which indicated a good correlation between the experimental inhibition values and the predicted free binding energy.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms21010005</identifier><identifier>PMID: 31861333</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Acetylcholinesterase ; Acetylcholinesterase - chemistry ; Alzheimer's disease ; Binding energy ; Binding Sites ; Catalytic Domain ; Chemistry Techniques, Synthetic ; Cholinergics ; Cholinesterase Inhibitors - chemical synthesis ; Cholinesterase Inhibitors - chemistry ; Cholinesterase Inhibitors - pharmacology ; Chromatography ; Computer applications ; Cycloaddition ; Drugs ; Enzyme Activation - drug effects ; Enzymes ; Free energy ; Humans ; Hybrids ; Hydrogen Bonding ; Isoxazoles - chemistry ; Kinetics ; Logistics ; Mathematical models ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Molecular modelling ; Molecular Structure ; Protein Binding ; Quinolines - chemistry ; Selectivity ; Structure-Activity Relationship</subject><ispartof>International journal of molecular sciences, 2019-12, Vol.21 (1), p.5</ispartof><rights>2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2019 by the authors. 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-293b0dbf433a98d6a35e1173bfab2efa2036287a3b8b3152b76fc8c77a886d373</citedby><cites>FETCH-LOGICAL-c412t-293b0dbf433a98d6a35e1173bfab2efa2036287a3b8b3152b76fc8c77a886d373</cites><orcidid>0000-0001-9624-7849 ; 0000-0003-4935-876X ; 0000-0003-0971-9081</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6981637/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6981637/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31861333$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rodríguez Núñez, Yeray A</creatorcontrib><creatorcontrib>Gutíerrez, Margarita</creatorcontrib><creatorcontrib>Alzate-Morales, Jans</creatorcontrib><creatorcontrib>Adasme-Carreño, Francisco</creatorcontrib><creatorcontrib>Güiza, Fausto M</creatorcontrib><creatorcontrib>Bernal, Cristian C</creatorcontrib><creatorcontrib>Bohórquez, Arnold R Romero</creatorcontrib><title>Tetrahydroquinoline-Isoxazole/Isoxazoline Hybrid Compounds as Potential Cholinesterases Inhibitors: Synthesis, Enzyme Inhibition Assays, and Molecular Modeling Studies</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>A series of 44 hybrid compounds that included in their structure tetrahydroquinoline (THQ) and isoxazole/isoxazoline moieties were synthesized through the 1,3-dipolar cycloaddition reaction (1,3-DC) from the corresponding
-allyl/propargyl THQs, previously obtained via cationic Povarov reaction. In vitro cholinergic enzymes inhibition potential of all compounds was tested. Enzyme inhibition assays showed that some hybrids exhibited significant potency to inhibit acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Especially, the hybrid compound 5n presented the more effective inhibition against AChE (4.24 µM) with an acceptable selectivity index versus BChE (SI: 5.19), while compound 6aa exhibited the greatest inhibition activity on BChE (3.97 µM) and a significant selectivity index against AChE (SI: 0.04). Kinetic studies were carried out for compounds with greater inhibitory activity of cholinesterases. Structure-activity relationships of the molecular hybrids were analyzed, through computational models using a molecular cross-docking algorithm and Molecular Mechanics/Generalized Born Surface Area (MM/GBSA) binding free energy approach, which indicated a good correlation between the experimental inhibition values and the predicted free binding energy.</description><subject>Acetylcholinesterase</subject><subject>Acetylcholinesterase - chemistry</subject><subject>Alzheimer's disease</subject><subject>Binding energy</subject><subject>Binding Sites</subject><subject>Catalytic Domain</subject><subject>Chemistry Techniques, Synthetic</subject><subject>Cholinergics</subject><subject>Cholinesterase Inhibitors - chemical synthesis</subject><subject>Cholinesterase Inhibitors - chemistry</subject><subject>Cholinesterase Inhibitors - pharmacology</subject><subject>Chromatography</subject><subject>Computer applications</subject><subject>Cycloaddition</subject><subject>Drugs</subject><subject>Enzyme Activation - drug effects</subject><subject>Enzymes</subject><subject>Free energy</subject><subject>Humans</subject><subject>Hybrids</subject><subject>Hydrogen Bonding</subject><subject>Isoxazoles - chemistry</subject><subject>Kinetics</subject><subject>Logistics</subject><subject>Mathematical models</subject><subject>Molecular Docking Simulation</subject><subject>Molecular Dynamics Simulation</subject><subject>Molecular modelling</subject><subject>Molecular Structure</subject><subject>Protein Binding</subject><subject>Quinolines - chemistry</subject><subject>Selectivity</subject><subject>Structure-Activity Relationship</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkk9P3DAQxaOqFVDKrefKUi89kOI_iZ30gIRWtKxEBRL0bNmxQ7xK7K0nqRq-EF8TL7Bo25OfPD89-81Mln0k-CtjNT5xqwEowQRjXL7JDkhBaY4xF2939H72HmCFMWW0rPeyfUYqThhjB9nDrR2j6mYTw-_J-dA7b_MlhL_qPvT2ZKvSLbqYdXQGLcKwDpM3gBSg6zBaPzrVo0X3RMFoowILaOk7p90YInxDN7MfOwsOjtG5v58Hu6264NEZgJpTRXmDfqY3m6lXMSljk98duhkn4yx8yN61qgd79HIeZr--n98uLvLLqx_Lxdll3hSEjjmtmcZGtwVjqq4MV6y0hAimW6WpbRXFjNNKKKYrzUhJteBtUzVCqKrihgl2mJ0--64nPVjTpHRR9XId3aDiLINy8t-Kd528C38kryvCnwy-vBhsOpr6IQcHje175W2YQKYR1IIJjouEfv4PXYUp-hRP0rKouKhLvDE8fqaaGACibV8_Q7DcbIDc3YCEf9oN8ApvR84eATE7scQ</recordid><startdate>20191218</startdate><enddate>20191218</enddate><creator>Rodríguez Núñez, Yeray A</creator><creator>Gutíerrez, Margarita</creator><creator>Alzate-Morales, Jans</creator><creator>Adasme-Carreño, Francisco</creator><creator>Güiza, Fausto M</creator><creator>Bernal, Cristian C</creator><creator>Bohórquez, Arnold R Romero</creator><general>MDPI AG</general><general>MDPI</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-9624-7849</orcidid><orcidid>https://orcid.org/0000-0003-4935-876X</orcidid><orcidid>https://orcid.org/0000-0003-0971-9081</orcidid></search><sort><creationdate>20191218</creationdate><title>Tetrahydroquinoline-Isoxazole/Isoxazoline Hybrid Compounds as Potential Cholinesterases Inhibitors: Synthesis, Enzyme Inhibition Assays, and Molecular Modeling Studies</title><author>Rodríguez Núñez, Yeray A ; Gutíerrez, Margarita ; Alzate-Morales, Jans ; Adasme-Carreño, Francisco ; Güiza, Fausto M ; Bernal, Cristian C ; Bohórquez, Arnold R Romero</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-293b0dbf433a98d6a35e1173bfab2efa2036287a3b8b3152b76fc8c77a886d373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Acetylcholinesterase</topic><topic>Acetylcholinesterase - chemistry</topic><topic>Alzheimer's disease</topic><topic>Binding energy</topic><topic>Binding Sites</topic><topic>Catalytic Domain</topic><topic>Chemistry Techniques, Synthetic</topic><topic>Cholinergics</topic><topic>Cholinesterase Inhibitors - chemical synthesis</topic><topic>Cholinesterase Inhibitors - chemistry</topic><topic>Cholinesterase Inhibitors - pharmacology</topic><topic>Chromatography</topic><topic>Computer applications</topic><topic>Cycloaddition</topic><topic>Drugs</topic><topic>Enzyme Activation - drug effects</topic><topic>Enzymes</topic><topic>Free energy</topic><topic>Humans</topic><topic>Hybrids</topic><topic>Hydrogen Bonding</topic><topic>Isoxazoles - chemistry</topic><topic>Kinetics</topic><topic>Logistics</topic><topic>Mathematical models</topic><topic>Molecular Docking Simulation</topic><topic>Molecular Dynamics Simulation</topic><topic>Molecular modelling</topic><topic>Molecular Structure</topic><topic>Protein Binding</topic><topic>Quinolines - chemistry</topic><topic>Selectivity</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rodríguez Núñez, Yeray A</creatorcontrib><creatorcontrib>Gutíerrez, Margarita</creatorcontrib><creatorcontrib>Alzate-Morales, Jans</creatorcontrib><creatorcontrib>Adasme-Carreño, Francisco</creatorcontrib><creatorcontrib>Güiza, Fausto M</creatorcontrib><creatorcontrib>Bernal, Cristian C</creatorcontrib><creatorcontrib>Bohórquez, Arnold R Romero</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rodríguez Núñez, Yeray A</au><au>Gutíerrez, Margarita</au><au>Alzate-Morales, Jans</au><au>Adasme-Carreño, Francisco</au><au>Güiza, Fausto M</au><au>Bernal, Cristian C</au><au>Bohórquez, Arnold R Romero</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tetrahydroquinoline-Isoxazole/Isoxazoline Hybrid Compounds as Potential Cholinesterases Inhibitors: Synthesis, Enzyme Inhibition Assays, and Molecular Modeling Studies</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2019-12-18</date><risdate>2019</risdate><volume>21</volume><issue>1</issue><spage>5</spage><pages>5-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>A series of 44 hybrid compounds that included in their structure tetrahydroquinoline (THQ) and isoxazole/isoxazoline moieties were synthesized through the 1,3-dipolar cycloaddition reaction (1,3-DC) from the corresponding
-allyl/propargyl THQs, previously obtained via cationic Povarov reaction. In vitro cholinergic enzymes inhibition potential of all compounds was tested. Enzyme inhibition assays showed that some hybrids exhibited significant potency to inhibit acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Especially, the hybrid compound 5n presented the more effective inhibition against AChE (4.24 µM) with an acceptable selectivity index versus BChE (SI: 5.19), while compound 6aa exhibited the greatest inhibition activity on BChE (3.97 µM) and a significant selectivity index against AChE (SI: 0.04). Kinetic studies were carried out for compounds with greater inhibitory activity of cholinesterases. Structure-activity relationships of the molecular hybrids were analyzed, through computational models using a molecular cross-docking algorithm and Molecular Mechanics/Generalized Born Surface Area (MM/GBSA) binding free energy approach, which indicated a good correlation between the experimental inhibition values and the predicted free binding energy.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>31861333</pmid><doi>10.3390/ijms21010005</doi><orcidid>https://orcid.org/0000-0001-9624-7849</orcidid><orcidid>https://orcid.org/0000-0003-4935-876X</orcidid><orcidid>https://orcid.org/0000-0003-0971-9081</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Acetylcholinesterase Acetylcholinesterase - chemistry Alzheimer's disease Binding energy Binding Sites Catalytic Domain Chemistry Techniques, Synthetic Cholinergics Cholinesterase Inhibitors - chemical synthesis Cholinesterase Inhibitors - chemistry Cholinesterase Inhibitors - pharmacology Chromatography Computer applications Cycloaddition Drugs Enzyme Activation - drug effects Enzymes Free energy Humans Hybrids Hydrogen Bonding Isoxazoles - chemistry Kinetics Logistics Mathematical models Molecular Docking Simulation Molecular Dynamics Simulation Molecular modelling Molecular Structure Protein Binding Quinolines - chemistry Selectivity Structure-Activity Relationship |
| title | Tetrahydroquinoline-Isoxazole/Isoxazoline Hybrid Compounds as Potential Cholinesterases Inhibitors: Synthesis, Enzyme Inhibition Assays, and Molecular Modeling Studies |
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