Design of self‐processing antimicrobial peptides for plant protection
Small antimicrobial peptides are excellent candidates for inclusion in self‐processing proteins that could be used to confer pathogen resistance in transgenic plants. Antimicrobial peptides as small as 22 amino acids in length have been designed to incorporate the residual amino acids left from prot...
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| Veröffentlicht in: | Letters in applied microbiology 2000-08, Vol.31 (2), p.163-168 |
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| container_end_page | 168 |
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| container_issue | 2 |
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| container_title | Letters in applied microbiology |
| container_volume | 31 |
| creator | Powell, W.A. Catranis, C.M. Maynard, C.A. |
| description | Small antimicrobial peptides are excellent candidates for inclusion in self‐processing proteins that could be used to confer pathogen resistance in transgenic plants. Antimicrobial peptides as small as 22 amino acids in length have been designed to incorporate the residual amino acids left from protein processing by the tobacco etch virus'(TEVs') NIa protease. Also, by minimizing the length of these peptides and the number of highly hydrophobic residues, haemolytic activity was reduced without affecting the peptide's antimicrobial activity. |
| doi_str_mv | 10.1046/j.1365-2672.2000.00782.x |
| format | Article |
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Antimicrobial peptides as small as 22 amino acids in length have been designed to incorporate the residual amino acids left from protein processing by the tobacco etch virus'(TEVs') NIa protease. 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Antimicrobial peptides as small as 22 amino acids in length have been designed to incorporate the residual amino acids left from protein processing by the tobacco etch virus'(TEVs') NIa protease. Also, by minimizing the length of these peptides and the number of highly hydrophobic residues, haemolytic activity was reduced without affecting the peptide's antimicrobial activity.</description><subject>Agrobacterium tumefaciens - drug effects</subject><subject>Amino Acid Sequence</subject><subject>Anti-Bacterial Agents</subject><subject>Anti-Infective Agents - chemistry</subject><subject>Anti-Infective Agents - pharmacology</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fusarium - drug effects</subject><subject>Hemolysis</subject><subject>Humans</subject><subject>Magainins</subject><subject>Methods. 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Technologies</subject><subject>Microbial Sensitivity Tests</subject><subject>Molecular Sequence Data</subject><subject>Peptides - chemistry</subject><subject>Peptides - pharmacology</subject><subject>Plant Diseases - microbiology</subject><subject>Plants, Genetically Modified - genetics</subject><subject>Protein engineering</subject><subject>Pseudomonas - drug effects</subject><subject>Xenopus Proteins</subject><issn>0266-8254</issn><issn>1472-765X</issn><issn>1365-2673</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM1q3DAQx0VJ6G7TvkLxoeRmZzT6NPQS0nzBhlxS6E14ZWnR4rVdy0s2tz5CnjFPUrm70NySkwb0m_nP_AjJKBQUuDxbF5RJkaNUWCAAFABKY7H7QOaUK8yVFL-OyBxQylyj4DPyKcZ1AjXF8iOZUSgVKqRzcv3DxbBqs85n0TX-5c9zP3TWxRjaVVa1Y9gEO3TLUDVZ7_ox1C5mvhuyvkmfWWJHZ8fQtZ_Jsa-a6L4c3hPy8-ry4eImX9xf316cL3LLkWOuS1lrptWSSskZWok1egBReyEl0NpVTtfaaq6k9q5k3EooS2EVQGkpFeyEnO7npujfWxdHswnRuiat47ptNAqRCcrZmyDVTKBElUC9B9OdMQ7Om34Im2p4MhTMZNuszWTbTLbNZNv8s212qfXrIWO73Lj6VeNebwK-HYAq2qrxQ9XaEP9z6UwK0wrf99hjaNzTu_PN4vwuFewvXSeaOQ</recordid><startdate>200008</startdate><enddate>200008</enddate><creator>Powell, W.A.</creator><creator>Catranis, C.M.</creator><creator>Maynard, C.A.</creator><general>Blackwell Science Ltd</general><general>Blackwell Science</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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>200008</creationdate><title>Design of self‐processing antimicrobial peptides for plant protection</title><author>Powell, W.A. ; Catranis, C.M. ; Maynard, C.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4242-896d8387b166432c62d2f005df56601deae8d8c84768fe934c60995c7009c1153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Agrobacterium tumefaciens - drug effects</topic><topic>Amino Acid Sequence</topic><topic>Anti-Bacterial Agents</topic><topic>Anti-Infective Agents - chemistry</topic><topic>Anti-Infective Agents - pharmacology</topic><topic>Antimicrobial Cationic Peptides - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fusarium - drug effects</topic><topic>Hemolysis</topic><topic>Humans</topic><topic>Magainins</topic><topic>Methods. Procedures. Technologies</topic><topic>Microbial Sensitivity Tests</topic><topic>Molecular Sequence Data</topic><topic>Peptides - chemistry</topic><topic>Peptides - pharmacology</topic><topic>Plant Diseases - microbiology</topic><topic>Plants, Genetically Modified - genetics</topic><topic>Protein engineering</topic><topic>Pseudomonas - drug effects</topic><topic>Xenopus Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Powell, W.A.</creatorcontrib><creatorcontrib>Catranis, C.M.</creatorcontrib><creatorcontrib>Maynard, C.A.</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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Letters in applied microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Powell, W.A.</au><au>Catranis, C.M.</au><au>Maynard, C.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Design of self‐processing antimicrobial peptides for plant protection</atitle><jtitle>Letters in applied microbiology</jtitle><addtitle>Lett Appl Microbiol</addtitle><date>2000-08</date><risdate>2000</risdate><volume>31</volume><issue>2</issue><spage>163</spage><epage>168</epage><pages>163-168</pages><issn>0266-8254</issn><eissn>1472-765X</eissn><eissn>1365-2673</eissn><coden>LAMIE7</coden><abstract>Small antimicrobial peptides are excellent candidates for inclusion in self‐processing proteins that could be used to confer pathogen resistance in transgenic plants. Antimicrobial peptides as small as 22 amino acids in length have been designed to incorporate the residual amino acids left from protein processing by the tobacco etch virus'(TEVs') NIa protease. Also, by minimizing the length of these peptides and the number of highly hydrophobic residues, haemolytic activity was reduced without affecting the peptide's antimicrobial activity.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>10972721</pmid><doi>10.1046/j.1365-2672.2000.00782.x</doi><tpages>6</tpages></addata></record> |
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| identifier | ISSN: 0266-8254 |
| ispartof | Letters in applied microbiology, 2000-08, Vol.31 (2), p.163-168 |
| issn | 0266-8254 1472-765X 1365-2673 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_72235143 |
| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Agrobacterium tumefaciens - drug effects Amino Acid Sequence Anti-Bacterial Agents Anti-Infective Agents - chemistry Anti-Infective Agents - pharmacology Antimicrobial Cationic Peptides - pharmacology Biological and medical sciences Biotechnology Fundamental and applied biological sciences. Psychology Fusarium - drug effects Hemolysis Humans Magainins Methods. Procedures. Technologies Microbial Sensitivity Tests Molecular Sequence Data Peptides - chemistry Peptides - pharmacology Plant Diseases - microbiology Plants, Genetically Modified - genetics Protein engineering Pseudomonas - drug effects Xenopus Proteins |
| title | Design of self‐processing antimicrobial peptides for plant protection |
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