1H NMR relaxation investigation of acetylcholinesterase inhibitors from huperzine A and derivative
The binding properties of huperzine A ( 1) with Torpediniforms Nacline acetylcholinesterase (TnAChE) were investigated by 1H NMR methods. The noselective, selective and double-selective spin-lattice relaxation rates were acquired in absent and present of TnAChE at a ratio [ligand]/[protein]=1:0.005....
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| Veröffentlicht in: | Bioorganic & medicinal chemistry letters 2004-03, Vol.14 (6), p.1585-1588 |
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| container_title | Bioorganic & medicinal chemistry letters |
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| creator | Li, Yiming Li, Qian Sun, Manchi Song, Guoqiang Jiang, Shanhao Zhu, Dayuan |
| description | The binding properties of huperzine A (
1) with
Torpediniforms Nacline acetylcholinesterase (TnAChE) were investigated by
1H NMR methods. The noselective, selective and double-selective spin-lattice relaxation rates were acquired in absent and present of TnAChE at a ratio [ligand]/[protein]=1:0.005. The selective relaxation rates shown protons of
1 had dipole–dipole interaction with protein active site protons. The motional correlation time of bound ligand was calculated by double-selective relaxation rate at
1 τ
2,3=40.5 ns at 298 K, which showed
1 had high affinity with TnAChE. The experiments give a possible method to use TnAChE to locate the new huperzine A derivatives as AChE inhibitors.
The binding properties of huperzine A (1) with
Torpediniforms Nacline acetylcholinesterase (TnAChE) were investigated by
1H NMR methods. The experiments give a possible method to use TnAChE to locate the new huperzine A derivatices as AChE inhibitors. |
| doi_str_mv | 10.1016/j.bmcl.2003.12.055 |
| format | Article |
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1) with
Torpediniforms Nacline acetylcholinesterase (TnAChE) were investigated by
1H NMR methods. The noselective, selective and double-selective spin-lattice relaxation rates were acquired in absent and present of TnAChE at a ratio [ligand]/[protein]=1:0.005. The selective relaxation rates shown protons of
1 had dipole–dipole interaction with protein active site protons. The motional correlation time of bound ligand was calculated by double-selective relaxation rate at
1 τ
2,3=40.5 ns at 298 K, which showed
1 had high affinity with TnAChE. The experiments give a possible method to use TnAChE to locate the new huperzine A derivatives as AChE inhibitors.
The binding properties of huperzine A (1) with
Torpediniforms Nacline acetylcholinesterase (TnAChE) were investigated by
1H NMR methods. The experiments give a possible method to use TnAChE to locate the new huperzine A derivatices as AChE inhibitors.</description><identifier>ISSN: 0960-894X</identifier><identifier>EISSN: 1464-3405</identifier><identifier>DOI: 10.1016/j.bmcl.2003.12.055</identifier><identifier>PMID: 15006409</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Acetylcholinesterase ; Alkaloids ; Animals ; Biological and medical sciences ; Cholinesterase Inhibitors - isolation & purification ; Cholinesterase Inhibitors - pharmacology ; Huperzia ; Huperzine A ; Hydrogen ; Magnetic Resonance Spectroscopy - methods ; Medical sciences ; Neuropharmacology ; NMR ; Pharmacology. Drug treatments ; Psychoanaleptics: cns stimulant, antidepressant agent, nootropic agent, mood stabilizer..., (alzheimer disease) ; Psychology. Psychoanalysis. Psychiatry ; Psychopharmacology ; Relaxation ; Sesquiterpenes - chemistry ; Sesquiterpenes - isolation & purification ; Sesquiterpenes - pharmacology ; Torpedo</subject><ispartof>Bioorganic & medicinal chemistry letters, 2004-03, Vol.14 (6), p.1585-1588</ispartof><rights>2004 Elsevier Ltd</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2299-77b8ad5fabd46d0cf228bf35e0ee5ccf6bc80b3258003ef7d67be7352ec5f6de3</citedby><cites>FETCH-LOGICAL-c2299-77b8ad5fabd46d0cf228bf35e0ee5ccf6bc80b3258003ef7d67be7352ec5f6de3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0960894X03013611$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15653878$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15006409$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Yiming</creatorcontrib><creatorcontrib>Li, Qian</creatorcontrib><creatorcontrib>Sun, Manchi</creatorcontrib><creatorcontrib>Song, Guoqiang</creatorcontrib><creatorcontrib>Jiang, Shanhao</creatorcontrib><creatorcontrib>Zhu, Dayuan</creatorcontrib><title>1H NMR relaxation investigation of acetylcholinesterase inhibitors from huperzine A and derivative</title><title>Bioorganic & medicinal chemistry letters</title><addtitle>Bioorg Med Chem Lett</addtitle><description>The binding properties of huperzine A (
1) with
Torpediniforms Nacline acetylcholinesterase (TnAChE) were investigated by
1H NMR methods. The noselective, selective and double-selective spin-lattice relaxation rates were acquired in absent and present of TnAChE at a ratio [ligand]/[protein]=1:0.005. The selective relaxation rates shown protons of
1 had dipole–dipole interaction with protein active site protons. The motional correlation time of bound ligand was calculated by double-selective relaxation rate at
1 τ
2,3=40.5 ns at 298 K, which showed
1 had high affinity with TnAChE. The experiments give a possible method to use TnAChE to locate the new huperzine A derivatives as AChE inhibitors.
The binding properties of huperzine A (1) with
Torpediniforms Nacline acetylcholinesterase (TnAChE) were investigated by
1H NMR methods. The experiments give a possible method to use TnAChE to locate the new huperzine A derivatices as AChE inhibitors.</description><subject>Acetylcholinesterase</subject><subject>Alkaloids</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cholinesterase Inhibitors - isolation & purification</subject><subject>Cholinesterase Inhibitors - pharmacology</subject><subject>Huperzia</subject><subject>Huperzine A</subject><subject>Hydrogen</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Medical sciences</subject><subject>Neuropharmacology</subject><subject>NMR</subject><subject>Pharmacology. Drug treatments</subject><subject>Psychoanaleptics: cns stimulant, antidepressant agent, nootropic agent, mood stabilizer..., (alzheimer disease)</subject><subject>Psychology. Psychoanalysis. Psychiatry</subject><subject>Psychopharmacology</subject><subject>Relaxation</subject><subject>Sesquiterpenes - chemistry</subject><subject>Sesquiterpenes - isolation & purification</subject><subject>Sesquiterpenes - pharmacology</subject><subject>Torpedo</subject><issn>0960-894X</issn><issn>1464-3405</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1v1DAQhi1ERbeFP8AB-QK3hLETO4nEpaqgRSqthEDiZvljzHqVxIudXdH-erzaleDEaTSaZ17NPIS8ZlAzYPL9pjaTHWsO0NSM1yDEM7JirWyrpgXxnKxgkFD1Q_vjnFzkvAFgLbTtC3LOBIBsYVgRw27p_ZevNOGof-slxJmGeY95CT-PXfRUW1weR7uOY5jLBJPOWKh1MGGJKVOf4kTXuy2mpwLQK6pnRx2msC8Re3xJzrweM7461Uvy_dPHb9e31d3Dzefrq7vKcj4MVdeZXjvhtXGtdGA9573xjUBAFNZ6aWwPpuGiL_-i75zsDHaN4GiFlw6bS_LumLtN8deuHKqmkC2Oo54x7rLqWMd6AbKA_AjaFHNO6NU2hUmnR8VAHcyqjTqYVQezinFVzJalN6f0nZnQ_V05qSzA2xOgs9WjT3q2If_DSdH0XV-4D0cOi4t9wKSyDThbdCGhXZSL4X93_AE6nplA</recordid><startdate>20040322</startdate><enddate>20040322</enddate><creator>Li, Yiming</creator><creator>Li, Qian</creator><creator>Sun, Manchi</creator><creator>Song, Guoqiang</creator><creator>Jiang, Shanhao</creator><creator>Zhu, Dayuan</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</scope><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></search><sort><creationdate>20040322</creationdate><title>1H NMR relaxation investigation of acetylcholinesterase inhibitors from huperzine A and derivative</title><author>Li, Yiming ; Li, Qian ; Sun, Manchi ; Song, Guoqiang ; Jiang, Shanhao ; Zhu, Dayuan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2299-77b8ad5fabd46d0cf228bf35e0ee5ccf6bc80b3258003ef7d67be7352ec5f6de3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Acetylcholinesterase</topic><topic>Alkaloids</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cholinesterase Inhibitors - isolation & purification</topic><topic>Cholinesterase Inhibitors - pharmacology</topic><topic>Huperzia</topic><topic>Huperzine A</topic><topic>Hydrogen</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>Medical sciences</topic><topic>Neuropharmacology</topic><topic>NMR</topic><topic>Pharmacology. Drug treatments</topic><topic>Psychoanaleptics: cns stimulant, antidepressant agent, nootropic agent, mood stabilizer..., (alzheimer disease)</topic><topic>Psychology. Psychoanalysis. Psychiatry</topic><topic>Psychopharmacology</topic><topic>Relaxation</topic><topic>Sesquiterpenes - chemistry</topic><topic>Sesquiterpenes - isolation & purification</topic><topic>Sesquiterpenes - pharmacology</topic><topic>Torpedo</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Yiming</creatorcontrib><creatorcontrib>Li, Qian</creatorcontrib><creatorcontrib>Sun, Manchi</creatorcontrib><creatorcontrib>Song, Guoqiang</creatorcontrib><creatorcontrib>Jiang, Shanhao</creatorcontrib><creatorcontrib>Zhu, Dayuan</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Yiming</au><au>Li, Qian</au><au>Sun, Manchi</au><au>Song, Guoqiang</au><au>Jiang, Shanhao</au><au>Zhu, Dayuan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>1H NMR relaxation investigation of acetylcholinesterase inhibitors from huperzine A and derivative</atitle><jtitle>Bioorganic & medicinal chemistry letters</jtitle><addtitle>Bioorg Med Chem Lett</addtitle><date>2004-03-22</date><risdate>2004</risdate><volume>14</volume><issue>6</issue><spage>1585</spage><epage>1588</epage><pages>1585-1588</pages><issn>0960-894X</issn><eissn>1464-3405</eissn><abstract>The binding properties of huperzine A (
1) with
Torpediniforms Nacline acetylcholinesterase (TnAChE) were investigated by
1H NMR methods. The noselective, selective and double-selective spin-lattice relaxation rates were acquired in absent and present of TnAChE at a ratio [ligand]/[protein]=1:0.005. The selective relaxation rates shown protons of
1 had dipole–dipole interaction with protein active site protons. The motional correlation time of bound ligand was calculated by double-selective relaxation rate at
1 τ
2,3=40.5 ns at 298 K, which showed
1 had high affinity with TnAChE. The experiments give a possible method to use TnAChE to locate the new huperzine A derivatives as AChE inhibitors.
The binding properties of huperzine A (1) with
Torpediniforms Nacline acetylcholinesterase (TnAChE) were investigated by
1H NMR methods. The experiments give a possible method to use TnAChE to locate the new huperzine A derivatices as AChE inhibitors.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>15006409</pmid><doi>10.1016/j.bmcl.2003.12.055</doi><tpages>4</tpages></addata></record> |
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| subjects | Acetylcholinesterase Alkaloids Animals Biological and medical sciences Cholinesterase Inhibitors - isolation & purification Cholinesterase Inhibitors - pharmacology Huperzia Huperzine A Hydrogen Magnetic Resonance Spectroscopy - methods Medical sciences Neuropharmacology NMR Pharmacology. Drug treatments Psychoanaleptics: cns stimulant, antidepressant agent, nootropic agent, mood stabilizer..., (alzheimer disease) Psychology. Psychoanalysis. Psychiatry Psychopharmacology Relaxation Sesquiterpenes - chemistry Sesquiterpenes - isolation & purification Sesquiterpenes - pharmacology Torpedo |
| title | 1H NMR relaxation investigation of acetylcholinesterase inhibitors from huperzine A and derivative |
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