A novel synthetic peptide from a tomato defensin exhibits antibacterial activities against Helicobacter pylori
Defensins are a class of cysteine‐rich proteins, which exert broad spectrum antimicrobial activity. In this work, we used a bioinformatic approach to identify putative defensins in the tomato genome. Fifteen proteins had a mature peptide that includes the well‐conserved tetradisulfide array. We sele...
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| Veröffentlicht in: | Journal of peptide science 2012-12, Vol.18 (12), p.755-762 |
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| creator | Rigano, M. M. Romanelli, A. Fulgione, A. Nocerino, N. D'Agostino, N. Avitabile, C. Frusciante, L. Barone, A. Capuano, F. Capparelli, R. |
| description | Defensins are a class of cysteine‐rich proteins, which exert broad spectrum antimicrobial activity. In this work, we used a bioinformatic approach to identify putative defensins in the tomato genome. Fifteen proteins had a mature peptide that includes the well‐conserved tetradisulfide array. We selected a representative member of the tomato defensin family; we chemically synthesized its γ‐motif and tested its antimicrobial activity. Here, we demonstrate that the synthetic peptide exhibits potent antibacterial activity against Gram‐positive bacteria, such as Staphylococcus aureus A170, Staphylococcus epidermidis, and Listeria monocytogenes, and Gram‐negative bacteria, including Salmonella enterica serovar Paratyphi, Escherichia coli, and Helicobacter pylori. In addition, the synthetic peptide shows minimal ( |
| doi_str_mv | 10.1002/psc.2462 |
| format | Article |
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In this work, we used a bioinformatic approach to identify putative defensins, a class of protein exerting broad spectrum antimicrobial activity, in the tomato genome. We selected a representative member of the tomato defensin family; we chemically synthesized its γ‐motif and tested its antimicrobial activity. Here, we demonstrate that the synthetic peptide exhibits antibacterial activity against Gram‐positive and Gram‐negative bacteria, including Helicobacter pylori. Moreover, the synthetic peptide shows minimal hemolytic activity, significant anti‐inflammatory properties, and absence of cytotoxic effects.</description><identifier>ISSN: 1075-2617</identifier><identifier>EISSN: 1099-1387</identifier><identifier>DOI: 10.1002/psc.2462</identifier><identifier>PMID: 23124812</identifier><identifier>CODEN: JPSIEI</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - pharmacology ; antimicrobial peptide ; Cell Line, Tumor ; defensin ; Defensins - chemistry ; Helicobacter pylori ; Helicobacter pylori - drug effects ; Hemolysis ; Humans ; Lycopersicon esculentum - chemistry ; Microbial Sensitivity Tests ; Molecular Sequence Data ; Peptide Fragments - chemistry ; Peptide Fragments - pharmacology ; Peptides ; Plant Proteins - chemistry ; tomato</subject><ispartof>Journal of peptide science, 2012-12, Vol.18 (12), p.755-762</ispartof><rights>Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4532-ec6c0738b5582f039d4fa37b8adfd508531d0dc75ccf9e3a6752ee9a6d98ae733</citedby><cites>FETCH-LOGICAL-c4532-ec6c0738b5582f039d4fa37b8adfd508531d0dc75ccf9e3a6752ee9a6d98ae733</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fpsc.2462$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fpsc.2462$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,782,786,1419,27933,27934,45583,45584</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23124812$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rigano, M. M.</creatorcontrib><creatorcontrib>Romanelli, A.</creatorcontrib><creatorcontrib>Fulgione, A.</creatorcontrib><creatorcontrib>Nocerino, N.</creatorcontrib><creatorcontrib>D'Agostino, N.</creatorcontrib><creatorcontrib>Avitabile, C.</creatorcontrib><creatorcontrib>Frusciante, L.</creatorcontrib><creatorcontrib>Barone, A.</creatorcontrib><creatorcontrib>Capuano, F.</creatorcontrib><creatorcontrib>Capparelli, R.</creatorcontrib><title>A novel synthetic peptide from a tomato defensin exhibits antibacterial activities against Helicobacter pylori</title><title>Journal of peptide science</title><addtitle>J. Pept. Sci</addtitle><description>Defensins are a class of cysteine‐rich proteins, which exert broad spectrum antimicrobial activity. In this work, we used a bioinformatic approach to identify putative defensins in the tomato genome. Fifteen proteins had a mature peptide that includes the well‐conserved tetradisulfide array. We selected a representative member of the tomato defensin family; we chemically synthesized its γ‐motif and tested its antimicrobial activity. Here, we demonstrate that the synthetic peptide exhibits potent antibacterial activity against Gram‐positive bacteria, such as Staphylococcus aureus A170, Staphylococcus epidermidis, and Listeria monocytogenes, and Gram‐negative bacteria, including Salmonella enterica serovar Paratyphi, Escherichia coli, and Helicobacter pylori. In addition, the synthetic peptide shows minimal (<5%) hemolytic activity and absence of cytotoxic effects against THP‐1 cells. Finally, SolyC exerts an anti‐inflammatory activity in vitro, as it downregulates the level of the proinflammatory cytokines TNF‐α and IFN‐γ. Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.
In this work, we used a bioinformatic approach to identify putative defensins, a class of protein exerting broad spectrum antimicrobial activity, in the tomato genome. We selected a representative member of the tomato defensin family; we chemically synthesized its γ‐motif and tested its antimicrobial activity. Here, we demonstrate that the synthetic peptide exhibits antibacterial activity against Gram‐positive and Gram‐negative bacteria, including Helicobacter pylori. Moreover, the synthetic peptide shows minimal hemolytic activity, significant anti‐inflammatory properties, and absence of cytotoxic effects.</description><subject>Amino Acid Sequence</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>antimicrobial peptide</subject><subject>Cell Line, Tumor</subject><subject>defensin</subject><subject>Defensins - chemistry</subject><subject>Helicobacter pylori</subject><subject>Helicobacter pylori - drug effects</subject><subject>Hemolysis</subject><subject>Humans</subject><subject>Lycopersicon esculentum - chemistry</subject><subject>Microbial Sensitivity Tests</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - pharmacology</subject><subject>Peptides</subject><subject>Plant Proteins - chemistry</subject><subject>tomato</subject><issn>1075-2617</issn><issn>1099-1387</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kV1rFDEUhoMotq6Cv0AC3ngzNR-bZHJZFvuhVQtVvAyZ5IxNnZlMk2zt_vtm2bWC4NU5cB6eczgvQq8pOaKEsPdzdkdsKdkTdEiJ1g3lrXq67ZVomKTqAL3I-YaQOhPyOTpgnLJlS9khmo7xFO9gwHkzlWsoweEZ5hI84D7FEVtc4mhLxB56mHKYMNxfhy6UjO1UQmddgRTsgGsT7kIJUAc_bZhywWcwBBd3CJ43Q0zhJXrW2yHDq31doO8nH76tzpqLr6fnq-OLxi0FZw046YjibSdEy3rCtV_2lquutb73grSCU0-8U8K5XgO3UgkGoK30urWgOF-gdzvvnOLtGnIxY8gOhsFOENfZUMnq3wSpSxbo7T_oTVynqV5nKBVUaq6F-it0KeacoDdzCqNNG0OJ2WZgagZmm0FF3-yF624E_wj-eXoFmh3wOwyw-a_IXF6t9sI9H3KB-0fepl9GKq6E-fHl1Kz4yaerz_qjueQPPBWgkg</recordid><startdate>201212</startdate><enddate>201212</enddate><creator>Rigano, M. M.</creator><creator>Romanelli, A.</creator><creator>Fulgione, A.</creator><creator>Nocerino, N.</creator><creator>D'Agostino, N.</creator><creator>Avitabile, C.</creator><creator>Frusciante, L.</creator><creator>Barone, A.</creator><creator>Capuano, F.</creator><creator>Capparelli, R.</creator><general>Blackwell Publishing Ltd</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</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>7QO</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>201212</creationdate><title>A novel synthetic peptide from a tomato defensin exhibits antibacterial activities against Helicobacter pylori</title><author>Rigano, M. M. ; Romanelli, A. ; Fulgione, A. ; Nocerino, N. ; D'Agostino, N. ; Avitabile, C. ; Frusciante, L. ; Barone, A. ; Capuano, F. ; Capparelli, R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4532-ec6c0738b5582f039d4fa37b8adfd508531d0dc75ccf9e3a6752ee9a6d98ae733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Sequence</topic><topic>Anti-Bacterial Agents - chemistry</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>antimicrobial peptide</topic><topic>Cell Line, Tumor</topic><topic>defensin</topic><topic>Defensins - chemistry</topic><topic>Helicobacter pylori</topic><topic>Helicobacter pylori - drug effects</topic><topic>Hemolysis</topic><topic>Humans</topic><topic>Lycopersicon esculentum - chemistry</topic><topic>Microbial Sensitivity Tests</topic><topic>Molecular Sequence Data</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - pharmacology</topic><topic>Peptides</topic><topic>Plant Proteins - chemistry</topic><topic>tomato</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rigano, M. M.</creatorcontrib><creatorcontrib>Romanelli, A.</creatorcontrib><creatorcontrib>Fulgione, A.</creatorcontrib><creatorcontrib>Nocerino, N.</creatorcontrib><creatorcontrib>D'Agostino, N.</creatorcontrib><creatorcontrib>Avitabile, C.</creatorcontrib><creatorcontrib>Frusciante, L.</creatorcontrib><creatorcontrib>Barone, A.</creatorcontrib><creatorcontrib>Capuano, F.</creatorcontrib><creatorcontrib>Capparelli, R.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of peptide science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rigano, M. M.</au><au>Romanelli, A.</au><au>Fulgione, A.</au><au>Nocerino, N.</au><au>D'Agostino, N.</au><au>Avitabile, C.</au><au>Frusciante, L.</au><au>Barone, A.</au><au>Capuano, F.</au><au>Capparelli, R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel synthetic peptide from a tomato defensin exhibits antibacterial activities against Helicobacter pylori</atitle><jtitle>Journal of peptide science</jtitle><addtitle>J. Pept. Sci</addtitle><date>2012-12</date><risdate>2012</risdate><volume>18</volume><issue>12</issue><spage>755</spage><epage>762</epage><pages>755-762</pages><issn>1075-2617</issn><eissn>1099-1387</eissn><coden>JPSIEI</coden><abstract>Defensins are a class of cysteine‐rich proteins, which exert broad spectrum antimicrobial activity. In this work, we used a bioinformatic approach to identify putative defensins in the tomato genome. Fifteen proteins had a mature peptide that includes the well‐conserved tetradisulfide array. We selected a representative member of the tomato defensin family; we chemically synthesized its γ‐motif and tested its antimicrobial activity. Here, we demonstrate that the synthetic peptide exhibits potent antibacterial activity against Gram‐positive bacteria, such as Staphylococcus aureus A170, Staphylococcus epidermidis, and Listeria monocytogenes, and Gram‐negative bacteria, including Salmonella enterica serovar Paratyphi, Escherichia coli, and Helicobacter pylori. In addition, the synthetic peptide shows minimal (<5%) hemolytic activity and absence of cytotoxic effects against THP‐1 cells. Finally, SolyC exerts an anti‐inflammatory activity in vitro, as it downregulates the level of the proinflammatory cytokines TNF‐α and IFN‐γ. Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.
In this work, we used a bioinformatic approach to identify putative defensins, a class of protein exerting broad spectrum antimicrobial activity, in the tomato genome. We selected a representative member of the tomato defensin family; we chemically synthesized its γ‐motif and tested its antimicrobial activity. Here, we demonstrate that the synthetic peptide exhibits antibacterial activity against Gram‐positive and Gram‐negative bacteria, including Helicobacter pylori. Moreover, the synthetic peptide shows minimal hemolytic activity, significant anti‐inflammatory properties, and absence of cytotoxic effects.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>23124812</pmid><doi>10.1002/psc.2462</doi><tpages>8</tpages></addata></record> |
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| subjects | Amino Acid Sequence Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology antimicrobial peptide Cell Line, Tumor defensin Defensins - chemistry Helicobacter pylori Helicobacter pylori - drug effects Hemolysis Humans Lycopersicon esculentum - chemistry Microbial Sensitivity Tests Molecular Sequence Data Peptide Fragments - chemistry Peptide Fragments - pharmacology Peptides Plant Proteins - chemistry tomato |
| title | A novel synthetic peptide from a tomato defensin exhibits antibacterial activities against Helicobacter pylori |
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