Design, synthesis and evaluation of new chromone-derived aminophosphonates as potential acetylcholinesterase inhibitor
A series of novel N-substituted α-aminophosphonates-bearing chromone moiety were synthesized and evaluated for acetylcholinesterase (AChE), butyrylcholinesterase (BuChE) activities and antioxidant properties. Porcine pancreatic lipase was employed as a catalyst. Inhibitory activity against AChE rang...
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| Veröffentlicht in: | Molecular diversity 2021-05, Vol.25 (2), p.811-825 |
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| creator | Shaikh, Sarfaraz Dhavan, Pratik Ramana, M. M. V. Jadhav, B. L. |
| description | A series of novel N-substituted α-aminophosphonates-bearing chromone moiety were synthesized and evaluated for acetylcholinesterase (AChE), butyrylcholinesterase (BuChE) activities and antioxidant properties. Porcine pancreatic lipase was employed as a catalyst. Inhibitory activity against AChE ranged between 0.103 and 5.781 µM, whereas for BuChE, activities ranged between 8.619 and 18.789 µM. The results show that among the various synthesized compounds, strongest AChE inhibition was found for the compound containing aliphatic amine analogs, while in case of BuChE, aromatic amines showed better activity as compared to aliphatic amines. Compound
4j
was found to be the most potent inhibitor of AChE with an IC
50
value of 0.103 ± 0.24 μM and inhibited AChE through mixed-type inhibition. Compound
4j
was twofolds more potent than tacrine, 35-folds potent than galantamine and 50-folds potent than rivastigmine. Also, docking study revealed that compound
4j
binds to both the peripheral anionic site and catalytic anionic site of AChE and BuChE. The antioxidant activities of synthesized compounds were performed against 2,2-diphenyl-1-picrylhydrazyl and hydrogen peroxide scavenging. DNA nicking activity of selected compounds also suggested that the compounds do not harm plasmid DNA pBR322. Compound
4j
also showed significant DNA damage protection activity.
Graphic abstract
Novel N-substituted α-aminophosphonates bearing chromone moiety were synthesized and evaluated for anti-acetylcholinesterase, anti-butyrylcholinesterase, antioxidant and DNA damage activities. |
| doi_str_mv | 10.1007/s11030-020-10060-y |
| format | Article |
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4j
was found to be the most potent inhibitor of AChE with an IC
50
value of 0.103 ± 0.24 μM and inhibited AChE through mixed-type inhibition. Compound
4j
was twofolds more potent than tacrine, 35-folds potent than galantamine and 50-folds potent than rivastigmine. Also, docking study revealed that compound
4j
binds to both the peripheral anionic site and catalytic anionic site of AChE and BuChE. The antioxidant activities of synthesized compounds were performed against 2,2-diphenyl-1-picrylhydrazyl and hydrogen peroxide scavenging. DNA nicking activity of selected compounds also suggested that the compounds do not harm plasmid DNA pBR322. Compound
4j
also showed significant DNA damage protection activity.
Graphic abstract
Novel N-substituted α-aminophosphonates bearing chromone moiety were synthesized and evaluated for anti-acetylcholinesterase, anti-butyrylcholinesterase, antioxidant and DNA damage activities.</description><identifier>ISSN: 1381-1991</identifier><identifier>EISSN: 1573-501X</identifier><identifier>DOI: 10.1007/s11030-020-10060-y</identifier><identifier>PMID: 32124162</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Antioxidants ; Biochemistry ; Biochemistry & Molecular Biology ; Biomedical and Life Sciences ; Chemistry ; Chemistry, Applied ; Chemistry, Medicinal ; Chemistry, Multidisciplinary ; DNA damage ; Life Sciences ; Life Sciences & Biomedicine ; Organic Chemistry ; Original Article ; Pharmacology & Pharmacy ; Pharmacy ; Physical Sciences ; Polymer Sciences ; Science & Technology</subject><ispartof>Molecular diversity, 2021-05, Vol.25 (2), p.811-825</ispartof><rights>Springer Nature Switzerland AG 2020</rights><rights>Springer Nature Switzerland AG 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>32</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000517917800001</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c375t-4c443eae30fea10a6864d1af3ee82fa795da6fd52dd869e218ccc9e4193b1de43</citedby><cites>FETCH-LOGICAL-c375t-4c443eae30fea10a6864d1af3ee82fa795da6fd52dd869e218ccc9e4193b1de43</cites><orcidid>0000-0002-2220-8019 ; 0000-0001-6082-2506</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/s11030-020-10060-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11030-020-10060-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,27928,27929,41492,42561,51323</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32124162$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shaikh, Sarfaraz</creatorcontrib><creatorcontrib>Dhavan, Pratik</creatorcontrib><creatorcontrib>Ramana, M. M. V.</creatorcontrib><creatorcontrib>Jadhav, B. L.</creatorcontrib><title>Design, synthesis and evaluation of new chromone-derived aminophosphonates as potential acetylcholinesterase inhibitor</title><title>Molecular diversity</title><addtitle>Mol Divers</addtitle><addtitle>MOL DIVERS</addtitle><addtitle>Mol Divers</addtitle><description>A series of novel N-substituted α-aminophosphonates-bearing chromone moiety were synthesized and evaluated for acetylcholinesterase (AChE), butyrylcholinesterase (BuChE) activities and antioxidant properties. Porcine pancreatic lipase was employed as a catalyst. Inhibitory activity against AChE ranged between 0.103 and 5.781 µM, whereas for BuChE, activities ranged between 8.619 and 18.789 µM. The results show that among the various synthesized compounds, strongest AChE inhibition was found for the compound containing aliphatic amine analogs, while in case of BuChE, aromatic amines showed better activity as compared to aliphatic amines. Compound
4j
was found to be the most potent inhibitor of AChE with an IC
50
value of 0.103 ± 0.24 μM and inhibited AChE through mixed-type inhibition. Compound
4j
was twofolds more potent than tacrine, 35-folds potent than galantamine and 50-folds potent than rivastigmine. Also, docking study revealed that compound
4j
binds to both the peripheral anionic site and catalytic anionic site of AChE and BuChE. The antioxidant activities of synthesized compounds were performed against 2,2-diphenyl-1-picrylhydrazyl and hydrogen peroxide scavenging. DNA nicking activity of selected compounds also suggested that the compounds do not harm plasmid DNA pBR322. Compound
4j
also showed significant DNA damage protection activity.
Graphic abstract
Novel N-substituted α-aminophosphonates bearing chromone moiety were synthesized and evaluated for anti-acetylcholinesterase, anti-butyrylcholinesterase, antioxidant and DNA damage activities.</description><subject>Antioxidants</subject><subject>Biochemistry</subject><subject>Biochemistry & Molecular Biology</subject><subject>Biomedical and Life Sciences</subject><subject>Chemistry</subject><subject>Chemistry, Applied</subject><subject>Chemistry, Medicinal</subject><subject>Chemistry, Multidisciplinary</subject><subject>DNA damage</subject><subject>Life Sciences</subject><subject>Life Sciences & Biomedicine</subject><subject>Organic Chemistry</subject><subject>Original Article</subject><subject>Pharmacology & Pharmacy</subject><subject>Pharmacy</subject><subject>Physical Sciences</subject><subject>Polymer Sciences</subject><subject>Science & Technology</subject><issn>1381-1991</issn><issn>1573-501X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>HGBXW</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkU9rFTEUxYMotn36BVxIwI1QR3OT-buU16qFghsFdyEvudNJmUmeSeaV-fbGN7WCi-Ii5AR-53JyDyGvgL0HxpoPEYAJVjDOivyuWbE8IadQNaKoGPx4mrVooYCugxNyFuMtYxkD8ZycCA68hJqfksMFRnvj3tG4uDRkHalyhuJBjbNK1jvqe-rwjuoh-Mk7LAwGe0BD1WSd3w8-5uNUwmyMdO8TumTVSJXGtIx68KN1GBMGFZFaN9idTT68IM96NUZ8eX9vyPdPl9-2X4rrr5-vth-vCy2aKhWlLkuBCgXrUQFTdVuXBlQvEFveq6arjKp7U3Fj2rpDDq3WusMSOrEDg6XYkLfr3H3wP-ecQ042ahxH5dDPUXLRsErUXckz-uYf9NbPweV0kle8rfMu8_I2hK-UDj7GgL3cBzupsEhg8ncrcm1F5lbksRW5ZNPr-9HzbkLzYPlTQwbOV-AOd76P2qLT-IAxxipoOmjarI4Z2v-ntzYde9z62aVsFas1ZtzdYPj7yUfy_wIUI7wT</recordid><startdate>20210501</startdate><enddate>20210501</enddate><creator>Shaikh, Sarfaraz</creator><creator>Dhavan, Pratik</creator><creator>Ramana, M. 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L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-4c443eae30fea10a6864d1af3ee82fa795da6fd52dd869e218ccc9e4193b1de43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Antioxidants</topic><topic>Biochemistry</topic><topic>Biochemistry & Molecular Biology</topic><topic>Biomedical and Life Sciences</topic><topic>Chemistry</topic><topic>Chemistry, Applied</topic><topic>Chemistry, Medicinal</topic><topic>Chemistry, Multidisciplinary</topic><topic>DNA damage</topic><topic>Life Sciences</topic><topic>Life Sciences & Biomedicine</topic><topic>Organic Chemistry</topic><topic>Original Article</topic><topic>Pharmacology & Pharmacy</topic><topic>Pharmacy</topic><topic>Physical Sciences</topic><topic>Polymer Sciences</topic><topic>Science & Technology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shaikh, Sarfaraz</creatorcontrib><creatorcontrib>Dhavan, Pratik</creatorcontrib><creatorcontrib>Ramana, M. 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M. V.</au><au>Jadhav, B. L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Design, synthesis and evaluation of new chromone-derived aminophosphonates as potential acetylcholinesterase inhibitor</atitle><jtitle>Molecular diversity</jtitle><stitle>Mol Divers</stitle><stitle>MOL DIVERS</stitle><addtitle>Mol Divers</addtitle><date>2021-05-01</date><risdate>2021</risdate><volume>25</volume><issue>2</issue><spage>811</spage><epage>825</epage><pages>811-825</pages><issn>1381-1991</issn><eissn>1573-501X</eissn><abstract>A series of novel N-substituted α-aminophosphonates-bearing chromone moiety were synthesized and evaluated for acetylcholinesterase (AChE), butyrylcholinesterase (BuChE) activities and antioxidant properties. Porcine pancreatic lipase was employed as a catalyst. Inhibitory activity against AChE ranged between 0.103 and 5.781 µM, whereas for BuChE, activities ranged between 8.619 and 18.789 µM. The results show that among the various synthesized compounds, strongest AChE inhibition was found for the compound containing aliphatic amine analogs, while in case of BuChE, aromatic amines showed better activity as compared to aliphatic amines. Compound
4j
was found to be the most potent inhibitor of AChE with an IC
50
value of 0.103 ± 0.24 μM and inhibited AChE through mixed-type inhibition. Compound
4j
was twofolds more potent than tacrine, 35-folds potent than galantamine and 50-folds potent than rivastigmine. Also, docking study revealed that compound
4j
binds to both the peripheral anionic site and catalytic anionic site of AChE and BuChE. The antioxidant activities of synthesized compounds were performed against 2,2-diphenyl-1-picrylhydrazyl and hydrogen peroxide scavenging. DNA nicking activity of selected compounds also suggested that the compounds do not harm plasmid DNA pBR322. Compound
4j
also showed significant DNA damage protection activity.
Graphic abstract
Novel N-substituted α-aminophosphonates bearing chromone moiety were synthesized and evaluated for anti-acetylcholinesterase, anti-butyrylcholinesterase, antioxidant and DNA damage activities.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>32124162</pmid><doi>10.1007/s11030-020-10060-y</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0002-2220-8019</orcidid><orcidid>https://orcid.org/0000-0001-6082-2506</orcidid></addata></record> |
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| language | eng |
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| source | SpringerNature Journals |
| subjects | Antioxidants Biochemistry Biochemistry & Molecular Biology Biomedical and Life Sciences Chemistry Chemistry, Applied Chemistry, Medicinal Chemistry, Multidisciplinary DNA damage Life Sciences Life Sciences & Biomedicine Organic Chemistry Original Article Pharmacology & Pharmacy Pharmacy Physical Sciences Polymer Sciences Science & Technology |
| title | Design, synthesis and evaluation of new chromone-derived aminophosphonates as potential acetylcholinesterase inhibitor |
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