Designed Amphiphilic β‑Sheet Peptides as Templates for Paraoxon Adsorption and Detection
Amphiphilic peptides were designed to fold into a β-sheet monolayer structure while presenting the catalytic triad residues of the enzyme, acetylcholinesterase (Glu, His, and Ser), to a solution containing the organophosphate, paraoxon. Three peptides, in which the catalytic triad residues were arra...
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Veröffentlicht in: | Langmuir 2013-06, Vol.29 (23), p.6840-6848 |
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description | Amphiphilic peptides were designed to fold into a β-sheet monolayer structure while presenting the catalytic triad residues of the enzyme, acetylcholinesterase (Glu, His, and Ser), to a solution containing the organophosphate, paraoxon. Three peptides, in which the catalytic triad residues were arranged in different orders along the strand, were generated to reveal potential differences in interactions with paraoxon as a function of the order of these amino acids. One additional peptide with amino acids introduced in random order was studied to highlight the contribution of the β-sheet secondary structure to any interactions with paraoxon. Langmuir isotherms, Brewster angle microscope at interfaces, and circular dichroism measurements in bulk showed that both the β-sheet conformation and the order of the amino acids along the strand influenced the interactions of paraoxon with the peptides. Compression isotherm curves as well as Brewster angle microscopy images provided evidence for enhanced adsorption of the paraoxon to the monolayers of peptides, which present neighboring Glu and Ser residues along the hydrophilic face of the β-strand. Circular dichroism revealed that the peptide most sensitive to interactions with paraoxon was that with the triad residues in the order Glu, Ser, and His, which appears to be appropriate for supporting a catalytic mechanism similar to that in the acetylcholinesterase enzyme. These rationally designed peptides may be further used for the development of technologies for organophosphate adsorption and detection. |
doi_str_mv | 10.1021/la401280e |
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Three peptides, in which the catalytic triad residues were arranged in different orders along the strand, were generated to reveal potential differences in interactions with paraoxon as a function of the order of these amino acids. One additional peptide with amino acids introduced in random order was studied to highlight the contribution of the β-sheet secondary structure to any interactions with paraoxon. Langmuir isotherms, Brewster angle microscope at interfaces, and circular dichroism measurements in bulk showed that both the β-sheet conformation and the order of the amino acids along the strand influenced the interactions of paraoxon with the peptides. Compression isotherm curves as well as Brewster angle microscopy images provided evidence for enhanced adsorption of the paraoxon to the monolayers of peptides, which present neighboring Glu and Ser residues along the hydrophilic face of the β-strand. Circular dichroism revealed that the peptide most sensitive to interactions with paraoxon was that with the triad residues in the order Glu, Ser, and His, which appears to be appropriate for supporting a catalytic mechanism similar to that in the acetylcholinesterase enzyme. These rationally designed peptides may be further used for the development of technologies for organophosphate adsorption and detection.</description><identifier>ISSN: 0743-7463</identifier><identifier>EISSN: 1520-5827</identifier><identifier>DOI: 10.1021/la401280e</identifier><identifier>PMID: 23631528</identifier><identifier>CODEN: LANGD5</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Adsorption ; Chemistry ; Exact sciences and technology ; General and physical chemistry ; Models, Molecular ; Paraoxon - chemistry ; Particle Size ; Peptides - chemical synthesis ; Peptides - chemistry ; Surface physical chemistry ; Surface Properties ; Surface-Active Agents - chemical synthesis ; Surface-Active Agents - chemistry</subject><ispartof>Langmuir, 2013-06, Vol.29 (23), p.6840-6848</ispartof><rights>Copyright © 2013 American Chemical Society</rights><rights>2014 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a345t-24ab6778d04e1670774f344c0247165074e6454eef394e3575e2991c0f2eb11c3</citedby><cites>FETCH-LOGICAL-a345t-24ab6778d04e1670774f344c0247165074e6454eef394e3575e2991c0f2eb11c3</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/la401280e$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/la401280e$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=27461657$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23631528$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yaakobi, Keren</creatorcontrib><creatorcontrib>Liebes-Peer, Yael</creatorcontrib><creatorcontrib>Kushmaro, Ariel</creatorcontrib><creatorcontrib>Rapaport, Hanna</creatorcontrib><title>Designed Amphiphilic β‑Sheet Peptides as Templates for Paraoxon Adsorption and Detection</title><title>Langmuir</title><addtitle>Langmuir</addtitle><description>Amphiphilic peptides were designed to fold into a β-sheet monolayer structure while presenting the catalytic triad residues of the enzyme, acetylcholinesterase (Glu, His, and Ser), to a solution containing the organophosphate, paraoxon. Three peptides, in which the catalytic triad residues were arranged in different orders along the strand, were generated to reveal potential differences in interactions with paraoxon as a function of the order of these amino acids. One additional peptide with amino acids introduced in random order was studied to highlight the contribution of the β-sheet secondary structure to any interactions with paraoxon. Langmuir isotherms, Brewster angle microscope at interfaces, and circular dichroism measurements in bulk showed that both the β-sheet conformation and the order of the amino acids along the strand influenced the interactions of paraoxon with the peptides. Compression isotherm curves as well as Brewster angle microscopy images provided evidence for enhanced adsorption of the paraoxon to the monolayers of peptides, which present neighboring Glu and Ser residues along the hydrophilic face of the β-strand. Circular dichroism revealed that the peptide most sensitive to interactions with paraoxon was that with the triad residues in the order Glu, Ser, and His, which appears to be appropriate for supporting a catalytic mechanism similar to that in the acetylcholinesterase enzyme. These rationally designed peptides may be further used for the development of technologies for organophosphate adsorption and detection.</description><subject>Adsorption</subject><subject>Chemistry</subject><subject>Exact sciences and technology</subject><subject>General and physical chemistry</subject><subject>Models, Molecular</subject><subject>Paraoxon - chemistry</subject><subject>Particle Size</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Surface physical chemistry</subject><subject>Surface Properties</subject><subject>Surface-Active Agents - chemical synthesis</subject><subject>Surface-Active Agents - chemistry</subject><issn>0743-7463</issn><issn>1520-5827</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0E1Kw0AUB_BBFFurCy8g2Qi6iM5XZpJlaf2CggXrykWYTl5sSpKJMwnozit4FQ_iITyJU1rtRhh48-DHezN_hI4JviCYkstScUxojGEH9UlEcRjFVO6iPpachZIL1kMHzi0xxgnjyT7qUSaYh3EfPY3BFc81ZMGwahaFP2Whg6_P7_ePhwVAG0yhaYsMXKBcMIOqKVXrm9zYYKqsMq-mDoaZM9Yrf1V1FoyhBb3qDtFerkoHR5s6QI_XV7PRbTi5v7kbDSehYjxqQ8rVXEgZZ5gDERJLyXPGucaUSyIi_wkQPOIAOUs4sEhGQJOEaJxTmBOi2QCdrec21rx04Nq0KpyGslQ1mM6lhAkRU4qF9PR8TbU1zlnI08YWlbJvKcHpKsv0L0tvTzZju3kF2Z_8Dc-D0w1QTqsyt6rWhds6n7x_v9w6pV26NJ2tfRr_LPwBCg2Htw</recordid><startdate>20130611</startdate><enddate>20130611</enddate><creator>Yaakobi, Keren</creator><creator>Liebes-Peer, Yael</creator><creator>Kushmaro, Ariel</creator><creator>Rapaport, Hanna</creator><general>American Chemical Society</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>20130611</creationdate><title>Designed Amphiphilic β‑Sheet Peptides as Templates for Paraoxon Adsorption and Detection</title><author>Yaakobi, Keren ; Liebes-Peer, Yael ; Kushmaro, Ariel ; Rapaport, Hanna</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a345t-24ab6778d04e1670774f344c0247165074e6454eef394e3575e2991c0f2eb11c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adsorption</topic><topic>Chemistry</topic><topic>Exact sciences and technology</topic><topic>General and physical chemistry</topic><topic>Models, Molecular</topic><topic>Paraoxon - chemistry</topic><topic>Particle Size</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Surface physical chemistry</topic><topic>Surface Properties</topic><topic>Surface-Active Agents - chemical synthesis</topic><topic>Surface-Active Agents - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yaakobi, Keren</creatorcontrib><creatorcontrib>Liebes-Peer, Yael</creatorcontrib><creatorcontrib>Kushmaro, Ariel</creatorcontrib><creatorcontrib>Rapaport, Hanna</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>Langmuir</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yaakobi, Keren</au><au>Liebes-Peer, Yael</au><au>Kushmaro, Ariel</au><au>Rapaport, Hanna</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Designed Amphiphilic β‑Sheet Peptides as Templates for Paraoxon Adsorption and Detection</atitle><jtitle>Langmuir</jtitle><addtitle>Langmuir</addtitle><date>2013-06-11</date><risdate>2013</risdate><volume>29</volume><issue>23</issue><spage>6840</spage><epage>6848</epage><pages>6840-6848</pages><issn>0743-7463</issn><eissn>1520-5827</eissn><coden>LANGD5</coden><abstract>Amphiphilic peptides were designed to fold into a β-sheet monolayer structure while presenting the catalytic triad residues of the enzyme, acetylcholinesterase (Glu, His, and Ser), to a solution containing the organophosphate, paraoxon. Three peptides, in which the catalytic triad residues were arranged in different orders along the strand, were generated to reveal potential differences in interactions with paraoxon as a function of the order of these amino acids. One additional peptide with amino acids introduced in random order was studied to highlight the contribution of the β-sheet secondary structure to any interactions with paraoxon. Langmuir isotherms, Brewster angle microscope at interfaces, and circular dichroism measurements in bulk showed that both the β-sheet conformation and the order of the amino acids along the strand influenced the interactions of paraoxon with the peptides. Compression isotherm curves as well as Brewster angle microscopy images provided evidence for enhanced adsorption of the paraoxon to the monolayers of peptides, which present neighboring Glu and Ser residues along the hydrophilic face of the β-strand. Circular dichroism revealed that the peptide most sensitive to interactions with paraoxon was that with the triad residues in the order Glu, Ser, and His, which appears to be appropriate for supporting a catalytic mechanism similar to that in the acetylcholinesterase enzyme. These rationally designed peptides may be further used for the development of technologies for organophosphate adsorption and detection.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>23631528</pmid><doi>10.1021/la401280e</doi><tpages>9</tpages></addata></record> |
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subjects | Adsorption Chemistry Exact sciences and technology General and physical chemistry Models, Molecular Paraoxon - chemistry Particle Size Peptides - chemical synthesis Peptides - chemistry Surface physical chemistry Surface Properties Surface-Active Agents - chemical synthesis Surface-Active Agents - chemistry |
title | Designed Amphiphilic β‑Sheet Peptides as Templates for Paraoxon Adsorption and Detection |
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