Oligopeptides as Mimic of Acetylcholinesterase: From the Rational Design to the Application in Solid-Phase Extraction for Pesticides
Three different peptides (His-Glu-Pro-Ser, His-Gly-Ser-Ala and Glu-Pro-Ser-Ala) were selected and tested to be used as affinity binding receptors for organophosphate and carbamate pesticides. The peptides were rationally designed by mimicking acetylcholinesterase active site. The simulated binding e...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2008-12, Vol.80 (23), p.9150-9156 |
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| creator | Mascini, M Sergi, M Monti, D Carlo, M. Del Compagnone, D |
| description | Three different peptides (His-Glu-Pro-Ser, His-Gly-Ser-Ala and Glu-Pro-Ser-Ala) were selected and tested to be used as affinity binding receptors for organophosphate and carbamate pesticides. The peptides were rationally designed by mimicking acetylcholinesterase active site. The simulated binding energy of the three tetrapeptides versus one model of organophosphate (paraoxon) and one of carbamate (carbaryl) pesticide was calculated; a good correlation between shape designed and binding score was obtained. The binding properties of the peptide−pesticide interaction were studied following the variation of UV−visible spectra in different solvents. The binding constants in water, which were nicely correlated with computational data, ranged from 506 (±115) to 36(±2) M−1. All the peptides had a 5-fold decrease in binding by changing solvent, going from water to less polar ethanol. The binding affinity suggested the use of these ligands as a preanalytical tool in extraction cartridges. The tetrapeptides efficiency was tested linking the peptides to two different supports. The cartridges prepared using His-Glu-Pro-Ser sequence was, as predicted, able to bind paraoxon and carbaryl with recovery values in the 72−88% range at pH 4.5. Intercolumn, interday RSD was in the 4−7% range. The columns were used for 80 cycles before losing retention ability. |
| doi_str_mv | 10.1021/ac801030j |
| format | Article |
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Del ; Compagnone, D</creator><creatorcontrib>Mascini, M ; Sergi, M ; Monti, D ; Carlo, M. Del ; Compagnone, D</creatorcontrib><description>Three different peptides (His-Glu-Pro-Ser, His-Gly-Ser-Ala and Glu-Pro-Ser-Ala) were selected and tested to be used as affinity binding receptors for organophosphate and carbamate pesticides. The peptides were rationally designed by mimicking acetylcholinesterase active site. The simulated binding energy of the three tetrapeptides versus one model of organophosphate (paraoxon) and one of carbamate (carbaryl) pesticide was calculated; a good correlation between shape designed and binding score was obtained. The binding properties of the peptide−pesticide interaction were studied following the variation of UV−visible spectra in different solvents. The binding constants in water, which were nicely correlated with computational data, ranged from 506 (±115) to 36(±2) M−1. All the peptides had a 5-fold decrease in binding by changing solvent, going from water to less polar ethanol. The binding affinity suggested the use of these ligands as a preanalytical tool in extraction cartridges. The tetrapeptides efficiency was tested linking the peptides to two different supports. The cartridges prepared using His-Glu-Pro-Ser sequence was, as predicted, able to bind paraoxon and carbaryl with recovery values in the 72−88% range at pH 4.5. Intercolumn, interday RSD was in the 4−7% range. The columns were used for 80 cycles before losing retention ability.</description><identifier>ISSN: 0003-2700</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/ac801030j</identifier><identifier>PMID: 19551938</identifier><identifier>CODEN: ANCHAM</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Acetylcholinesterase - chemistry ; Acetylcholinesterase - metabolism ; Amino Acid Sequence ; Analytical biochemistry: general aspects, technics, instrumentation ; Analytical chemistry ; Analytical, structural and metabolic biochemistry ; Binding sites ; Biological and medical sciences ; Biomimetics ; Carbamates - isolation & purification ; Carbamates - metabolism ; Chemistry ; Exact sciences and technology ; Extraction processes ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Oligopeptides - chemical synthesis ; Oligopeptides - chemistry ; Oligopeptides - metabolism ; Organophosphates - isolation & purification ; Organophosphates - metabolism ; Peptides ; Pesticides ; Pesticides - isolation & purification ; Pesticides - metabolism ; Protein Binding ; Sensitivity and Specificity ; Simulation ; Solid Phase Extraction - methods ; Spectrometric and optical methods ; Spectrophotometry</subject><ispartof>Analytical chemistry (Washington), 2008-12, Vol.80 (23), p.9150-9156</ispartof><rights>Copyright © 2008 American Chemical Society</rights><rights>2009 INIST-CNRS</rights><rights>Copyright American Chemical Society Dec 1, 2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a408t-c25cb5aee65d12b1059e8614f7e22e827e0fff5ae5d3d606cb3ef6978d05c7b73</citedby><cites>FETCH-LOGICAL-a408t-c25cb5aee65d12b1059e8614f7e22e827e0fff5ae5d3d606cb3ef6978d05c7b73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ac801030j$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ac801030j$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20940577$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19551938$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mascini, M</creatorcontrib><creatorcontrib>Sergi, M</creatorcontrib><creatorcontrib>Monti, D</creatorcontrib><creatorcontrib>Carlo, M. Del</creatorcontrib><creatorcontrib>Compagnone, D</creatorcontrib><title>Oligopeptides as Mimic of Acetylcholinesterase: From the Rational Design to the Application in Solid-Phase Extraction for Pesticides</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>Three different peptides (His-Glu-Pro-Ser, His-Gly-Ser-Ala and Glu-Pro-Ser-Ala) were selected and tested to be used as affinity binding receptors for organophosphate and carbamate pesticides. The peptides were rationally designed by mimicking acetylcholinesterase active site. The simulated binding energy of the three tetrapeptides versus one model of organophosphate (paraoxon) and one of carbamate (carbaryl) pesticide was calculated; a good correlation between shape designed and binding score was obtained. The binding properties of the peptide−pesticide interaction were studied following the variation of UV−visible spectra in different solvents. The binding constants in water, which were nicely correlated with computational data, ranged from 506 (±115) to 36(±2) M−1. All the peptides had a 5-fold decrease in binding by changing solvent, going from water to less polar ethanol. The binding affinity suggested the use of these ligands as a preanalytical tool in extraction cartridges. The tetrapeptides efficiency was tested linking the peptides to two different supports. The cartridges prepared using His-Glu-Pro-Ser sequence was, as predicted, able to bind paraoxon and carbaryl with recovery values in the 72−88% range at pH 4.5. Intercolumn, interday RSD was in the 4−7% range. The columns were used for 80 cycles before losing retention ability.</description><subject>Acetylcholinesterase - chemistry</subject><subject>Acetylcholinesterase - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Analytical biochemistry: general aspects, technics, instrumentation</subject><subject>Analytical chemistry</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Binding sites</subject><subject>Biological and medical sciences</subject><subject>Biomimetics</subject><subject>Carbamates - isolation & purification</subject><subject>Carbamates - metabolism</subject><subject>Chemistry</subject><subject>Exact sciences and technology</subject><subject>Extraction processes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Oligopeptides - chemical synthesis</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - metabolism</subject><subject>Organophosphates - isolation & purification</subject><subject>Organophosphates - metabolism</subject><subject>Peptides</subject><subject>Pesticides</subject><subject>Pesticides - isolation & purification</subject><subject>Pesticides - metabolism</subject><subject>Protein Binding</subject><subject>Sensitivity and Specificity</subject><subject>Simulation</subject><subject>Solid Phase Extraction - methods</subject><subject>Spectrometric and optical methods</subject><subject>Spectrophotometry</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkE1vEzEQhi0EomnhwB9AFhIHDgtjb_yx3ELTlo9AI1ouXCyv126cbtaLvZHaOz8c50PJgdNI8z7zzsyL0CsC7wlQ8kEbCQRKWD5BI8IoFFxK-hSNAKAsqAA4QacpLQEIAcKfoxNSMUaqUo7Q3-vW34Xe9oNvbMI64e9-5Q0ODk-MHR5bswit72wabNTJfsSXMazwsLD4px586HSLpzb5uw4PYdue9H3rzVbDvsM3ebop5os8iy8ehqjNVnEh4nk29Waz9gV65nSb7Mt9PUO_Li9uzz8Xs-urL-eTWaHHIIfCUGZqpq3lrCG0JsAqKzkZO2EptZIKC865DLCmbDhwU5fW8UrIBpgRtSjP0Judbx_Dn3Ver5ZhHfMPSVEipBwTBhl6t4NMDClF61Qf_UrHR0VAbeJWh7gz-3pvuK5XtjmS-3wz8HYP6GR066LujE8HjkI1BiY2lxU7zuegHw66jveKi1IwdTu_UbPppx_82--p-nr01SYdn_j_wH-WmqPj</recordid><startdate>20081201</startdate><enddate>20081201</enddate><creator>Mascini, M</creator><creator>Sergi, M</creator><creator>Monti, D</creator><creator>Carlo, M. Del</creator><creator>Compagnone, D</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U7</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope></search><sort><creationdate>20081201</creationdate><title>Oligopeptides as Mimic of Acetylcholinesterase: From the Rational Design to the Application in Solid-Phase Extraction for Pesticides</title><author>Mascini, M ; Sergi, M ; Monti, D ; Carlo, M. Del ; Compagnone, D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a408t-c25cb5aee65d12b1059e8614f7e22e827e0fff5ae5d3d606cb3ef6978d05c7b73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Acetylcholinesterase - chemistry</topic><topic>Acetylcholinesterase - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Analytical biochemistry: general aspects, technics, instrumentation</topic><topic>Analytical chemistry</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Binding sites</topic><topic>Biological and medical sciences</topic><topic>Biomimetics</topic><topic>Carbamates - isolation & purification</topic><topic>Carbamates - metabolism</topic><topic>Chemistry</topic><topic>Exact sciences and technology</topic><topic>Extraction processes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Oligopeptides - chemical synthesis</topic><topic>Oligopeptides - chemistry</topic><topic>Oligopeptides - metabolism</topic><topic>Organophosphates - isolation & purification</topic><topic>Organophosphates - metabolism</topic><topic>Peptides</topic><topic>Pesticides</topic><topic>Pesticides - isolation & purification</topic><topic>Pesticides - metabolism</topic><topic>Protein Binding</topic><topic>Sensitivity and Specificity</topic><topic>Simulation</topic><topic>Solid Phase Extraction - methods</topic><topic>Spectrometric and optical methods</topic><topic>Spectrophotometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mascini, M</creatorcontrib><creatorcontrib>Sergi, M</creatorcontrib><creatorcontrib>Monti, D</creatorcontrib><creatorcontrib>Carlo, M. 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Del</au><au>Compagnone, D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oligopeptides as Mimic of Acetylcholinesterase: From the Rational Design to the Application in Solid-Phase Extraction for Pesticides</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>2008-12-01</date><risdate>2008</risdate><volume>80</volume><issue>23</issue><spage>9150</spage><epage>9156</epage><pages>9150-9156</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>Three different peptides (His-Glu-Pro-Ser, His-Gly-Ser-Ala and Glu-Pro-Ser-Ala) were selected and tested to be used as affinity binding receptors for organophosphate and carbamate pesticides. The peptides were rationally designed by mimicking acetylcholinesterase active site. The simulated binding energy of the three tetrapeptides versus one model of organophosphate (paraoxon) and one of carbamate (carbaryl) pesticide was calculated; a good correlation between shape designed and binding score was obtained. The binding properties of the peptide−pesticide interaction were studied following the variation of UV−visible spectra in different solvents. The binding constants in water, which were nicely correlated with computational data, ranged from 506 (±115) to 36(±2) M−1. All the peptides had a 5-fold decrease in binding by changing solvent, going from water to less polar ethanol. The binding affinity suggested the use of these ligands as a preanalytical tool in extraction cartridges. The tetrapeptides efficiency was tested linking the peptides to two different supports. The cartridges prepared using His-Glu-Pro-Ser sequence was, as predicted, able to bind paraoxon and carbaryl with recovery values in the 72−88% range at pH 4.5. Intercolumn, interday RSD was in the 4−7% range. The columns were used for 80 cycles before losing retention ability.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>19551938</pmid><doi>10.1021/ac801030j</doi><tpages>7</tpages></addata></record> |
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| subjects | Acetylcholinesterase - chemistry Acetylcholinesterase - metabolism Amino Acid Sequence Analytical biochemistry: general aspects, technics, instrumentation Analytical chemistry Analytical, structural and metabolic biochemistry Binding sites Biological and medical sciences Biomimetics Carbamates - isolation & purification Carbamates - metabolism Chemistry Exact sciences and technology Extraction processes Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Oligopeptides - chemical synthesis Oligopeptides - chemistry Oligopeptides - metabolism Organophosphates - isolation & purification Organophosphates - metabolism Peptides Pesticides Pesticides - isolation & purification Pesticides - metabolism Protein Binding Sensitivity and Specificity Simulation Solid Phase Extraction - methods Spectrometric and optical methods Spectrophotometry |
| title | Oligopeptides as Mimic of Acetylcholinesterase: From the Rational Design to the Application in Solid-Phase Extraction for Pesticides |
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