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Antimicrobial Peptides for Detection of Bacteria in Biosensor Assays
Bacteria, plants, and higher and lower animals have evolved an innate immune system as a first line of defense against microbial invasion. Some of these organisms produce antimicrobial peptides (AMPs) as a part of this chemical immune system. AMPs exert their antimicrobial activity by binding to com...
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Published in: | Analytical chemistry (Washington) 2005-10, Vol.77 (19), p.6504-6508 |
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description | Bacteria, plants, and higher and lower animals have evolved an innate immune system as a first line of defense against microbial invasion. Some of these organisms produce antimicrobial peptides (AMPs) as a part of this chemical immune system. AMPs exert their antimicrobial activity by binding to components of the microbe's surface and disrupting the membrane. The overall goal of this study was to apply the AMP magainin I as a recognition element for Escherichia coli O157:H7 and Salmonella typhimurium detection on an array-based biosensor. We immobilized magainin I on silanized glass slides using biotin−avidin chemistry, as well as through direct covalent attachment. Cy5-labeled, heat-killed cells were used to demonstrate that the immobilized magainin I can bind Salmonella with detection limits similar to analogous antibody-based assays. Detection limits for E. coli were higher than in analogous antibody-based assays, but it is expected that other AMPs may possess higher affinities for this target. The results showed that both specific and nonspecific binding strongly depend on the method used for peptide immobilization. Direct attachment of magainin to the substrate surface not only decreased nonspecific cell binding but also resulted in improved detection limits for both Salmonella and E. coli. |
doi_str_mv | 10.1021/ac050639r |
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Some of these organisms produce antimicrobial peptides (AMPs) as a part of this chemical immune system. AMPs exert their antimicrobial activity by binding to components of the microbe's surface and disrupting the membrane. The overall goal of this study was to apply the AMP magainin I as a recognition element for Escherichia coli O157:H7 and Salmonella typhimurium detection on an array-based biosensor. We immobilized magainin I on silanized glass slides using biotin−avidin chemistry, as well as through direct covalent attachment. Cy5-labeled, heat-killed cells were used to demonstrate that the immobilized magainin I can bind Salmonella with detection limits similar to analogous antibody-based assays. Detection limits for E. coli were higher than in analogous antibody-based assays, but it is expected that other AMPs may possess higher affinities for this target. The results showed that both specific and nonspecific binding strongly depend on the method used for peptide immobilization. Direct attachment of magainin to the substrate surface not only decreased nonspecific cell binding but also resulted in improved detection limits for both Salmonella and E. coli.</description><identifier>ISSN: 0003-2700</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/ac050639r</identifier><identifier>PMID: 16194120</identifier><identifier>CODEN: ANCHAM</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical chemistry ; Anti-Infective Agents - analysis ; Anti-Infective Agents - metabolism ; Antimicrobial Cationic Peptides - analysis ; Antimicrobial Cationic Peptides - metabolism ; Bacteria ; Biological and medical sciences ; Biosensing Techniques - methods ; Biosensors ; Biotechnology ; Chemistry ; Escherichia coli ; Escherichia coli - isolation & purification ; Escherichia coli - metabolism ; Exact sciences and technology ; Fundamental and applied biological sciences. Psychology ; General, instrumentation ; Immune system ; Methods. Procedures. Technologies ; Peptides ; Salmonella typhimurium ; Salmonella typhimurium - isolation & purification ; Salmonella typhimurium - metabolism ; Various methods and equipments</subject><ispartof>Analytical chemistry (Washington), 2005-10, Vol.77 (19), p.6504-6508</ispartof><rights>Copyright © 2005 American Chemical Society</rights><rights>2006 INIST-CNRS</rights><rights>Copyright American Chemical Society Oct 1, 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a476t-c84f05bfea0a7f7ed8b2d5ec8db403377df2615a5f6125111348bd521c741db33</citedby><cites>FETCH-LOGICAL-a476t-c84f05bfea0a7f7ed8b2d5ec8db403377df2615a5f6125111348bd521c741db33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17175658$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16194120$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kulagina, Nadezhda V</creatorcontrib><creatorcontrib>Lassman, Michael E</creatorcontrib><creatorcontrib>Ligler, Frances S</creatorcontrib><creatorcontrib>Taitt, Chris Rowe</creatorcontrib><title>Antimicrobial Peptides for Detection of Bacteria in Biosensor Assays</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>Bacteria, plants, and higher and lower animals have evolved an innate immune system as a first line of defense against microbial invasion. Some of these organisms produce antimicrobial peptides (AMPs) as a part of this chemical immune system. AMPs exert their antimicrobial activity by binding to components of the microbe's surface and disrupting the membrane. The overall goal of this study was to apply the AMP magainin I as a recognition element for Escherichia coli O157:H7 and Salmonella typhimurium detection on an array-based biosensor. We immobilized magainin I on silanized glass slides using biotin−avidin chemistry, as well as through direct covalent attachment. Cy5-labeled, heat-killed cells were used to demonstrate that the immobilized magainin I can bind Salmonella with detection limits similar to analogous antibody-based assays. Detection limits for E. coli were higher than in analogous antibody-based assays, but it is expected that other AMPs may possess higher affinities for this target. The results showed that both specific and nonspecific binding strongly depend on the method used for peptide immobilization. Direct attachment of magainin to the substrate surface not only decreased nonspecific cell binding but also resulted in improved detection limits for both Salmonella and E. coli.</description><subject>Analytical chemistry</subject><subject>Anti-Infective Agents - analysis</subject><subject>Anti-Infective Agents - metabolism</subject><subject>Antimicrobial Cationic Peptides - analysis</subject><subject>Antimicrobial Cationic Peptides - metabolism</subject><subject>Bacteria</subject><subject>Biological and medical sciences</subject><subject>Biosensing Techniques - methods</subject><subject>Biosensors</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Escherichia coli</subject><subject>Escherichia coli - isolation & purification</subject><subject>Escherichia coli - metabolism</subject><subject>Exact sciences and technology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General, instrumentation</subject><subject>Immune system</subject><subject>Methods. Procedures. Technologies</subject><subject>Peptides</subject><subject>Salmonella typhimurium</subject><subject>Salmonella typhimurium - isolation & purification</subject><subject>Salmonella typhimurium - metabolism</subject><subject>Various methods and equipments</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqF0Utr3DAQB3BRWppt2kO_QDGFFHpwOiNZDx83m75gQzc07aEXIcsSKPHaG40Xkm9fh12y0Bx6msP8-DMPxt4inCJw_OQ8SFCizs_YDCWHUhnDn7MZAIiSa4Aj9oroGgARUL1kR6iwrpDDjJ3P-zGtk89Dk1xXrMJmTG2gIg65OA9j8GMa-mKIxZnzY8jJFakvztJAoaeJzIncPb1mL6LrKLzZ12P268vnq8W3cvnj6_fFfFm6Squx9KaKIJsYHDgddWhNw1sZvGmbCoTQuo1coXQyKuQSEUVlmlZy9LrCthHimH3Y5W7ycLsNNNp1Ih-6zvVh2JJVRglT8-q_EGutQQuY4Pt_4PWwzf20hOWoa0Bj9IQ-7tB0JaIcot3ktHb53iLYhwfYxwdM9t0-cNusQ3uQ-4tP4GQPHHnXxex6n-jgNGqppJlcuXOJxnD32Hf5xiottLRXq592BX8WF7-XYC8Puc7TYYmnA_4FPBGmiA</recordid><startdate>20051001</startdate><enddate>20051001</enddate><creator>Kulagina, Nadezhda V</creator><creator>Lassman, Michael E</creator><creator>Ligler, Frances S</creator><creator>Taitt, Chris Rowe</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><scope>7QL</scope><scope>7T7</scope><scope>7X8</scope></search><sort><creationdate>20051001</creationdate><title>Antimicrobial Peptides for Detection of Bacteria in Biosensor Assays</title><author>Kulagina, Nadezhda V ; Lassman, Michael E ; Ligler, Frances S ; Taitt, Chris Rowe</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a476t-c84f05bfea0a7f7ed8b2d5ec8db403377df2615a5f6125111348bd521c741db33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Analytical chemistry</topic><topic>Anti-Infective Agents - analysis</topic><topic>Anti-Infective Agents - metabolism</topic><topic>Antimicrobial Cationic Peptides - analysis</topic><topic>Antimicrobial Cationic Peptides - metabolism</topic><topic>Bacteria</topic><topic>Biological and medical sciences</topic><topic>Biosensing Techniques - methods</topic><topic>Biosensors</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Escherichia coli</topic><topic>Escherichia coli - isolation & purification</topic><topic>Escherichia coli - metabolism</topic><topic>Exact sciences and technology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General, instrumentation</topic><topic>Immune system</topic><topic>Methods. Procedures. Technologies</topic><topic>Peptides</topic><topic>Salmonella typhimurium</topic><topic>Salmonella typhimurium - isolation & purification</topic><topic>Salmonella typhimurium - metabolism</topic><topic>Various methods and equipments</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kulagina, Nadezhda V</creatorcontrib><creatorcontrib>Lassman, Michael E</creatorcontrib><creatorcontrib>Ligler, Frances S</creatorcontrib><creatorcontrib>Taitt, Chris Rowe</creatorcontrib><collection>Istex</collection><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>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical chemistry (Washington)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kulagina, Nadezhda V</au><au>Lassman, Michael E</au><au>Ligler, Frances S</au><au>Taitt, Chris Rowe</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antimicrobial Peptides for Detection of Bacteria in Biosensor Assays</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>2005-10-01</date><risdate>2005</risdate><volume>77</volume><issue>19</issue><spage>6504</spage><epage>6508</epage><pages>6504-6508</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>Bacteria, plants, and higher and lower animals have evolved an innate immune system as a first line of defense against microbial invasion. Some of these organisms produce antimicrobial peptides (AMPs) as a part of this chemical immune system. AMPs exert their antimicrobial activity by binding to components of the microbe's surface and disrupting the membrane. The overall goal of this study was to apply the AMP magainin I as a recognition element for Escherichia coli O157:H7 and Salmonella typhimurium detection on an array-based biosensor. We immobilized magainin I on silanized glass slides using biotin−avidin chemistry, as well as through direct covalent attachment. Cy5-labeled, heat-killed cells were used to demonstrate that the immobilized magainin I can bind Salmonella with detection limits similar to analogous antibody-based assays. Detection limits for E. coli were higher than in analogous antibody-based assays, but it is expected that other AMPs may possess higher affinities for this target. The results showed that both specific and nonspecific binding strongly depend on the method used for peptide immobilization. Direct attachment of magainin to the substrate surface not only decreased nonspecific cell binding but also resulted in improved detection limits for both Salmonella and E. coli.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>16194120</pmid><doi>10.1021/ac050639r</doi><tpages>5</tpages></addata></record> |
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subjects | Analytical chemistry Anti-Infective Agents - analysis Anti-Infective Agents - metabolism Antimicrobial Cationic Peptides - analysis Antimicrobial Cationic Peptides - metabolism Bacteria Biological and medical sciences Biosensing Techniques - methods Biosensors Biotechnology Chemistry Escherichia coli Escherichia coli - isolation & purification Escherichia coli - metabolism Exact sciences and technology Fundamental and applied biological sciences. Psychology General, instrumentation Immune system Methods. Procedures. Technologies Peptides Salmonella typhimurium Salmonella typhimurium - isolation & purification Salmonella typhimurium - metabolism Various methods and equipments |
title | Antimicrobial Peptides for Detection of Bacteria in Biosensor Assays |
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