Minimal antimicrobial peptidic sequence from hemoglobin alpha-chain: KYR
► Peptides derived from α 107–141 were antibacterial whatever the bacterial species. ► The most active peptide is the shortest one: α 137–141. ► Shortest the sequence of the peptide is, lowest the MIC is. ► KYR sequence is the minimal antimicrobial sequence from the hemoglobin α-chain. ► These activ...
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| Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2011-04, Vol.32 (4), p.633-638 |
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| creator | Catiau, Lucie Traisnel, Johnatan Delval-Dubois, Véronique Chihib, Nour-Eddine Guillochon, Didier Nedjar-Arroume, Naïma |
| description | ► Peptides derived from α 107–141 were antibacterial whatever the bacterial species. ► The most active peptide is the shortest one: α 137–141. ► Shortest the sequence of the peptide is, lowest the MIC is. ► KYR sequence is the minimal antimicrobial sequence from the hemoglobin α-chain. ► These active peptides were able to interact with cellular membrane.
Hemoglobin is an animal protein described as a source of biologically active peptides. Peptic digestion of bovine hemoglobin alpha-chain allowed obtaining peptide fractions with antimicrobial activity. These peptides were purified by reverse-phase High-Performance Liquid Chromatography (HPLC) and characterized by mass spectrometry. The minimal inhibitory concentration and mode of action of these peptides were studied against five bacterial strains including
Escherichia coli and
Salmonella enteritidis as Gram-negative bacteria and
Listeria innocua, Micrococcus luteus and
Staphylococcus aureus as Gram-positive bacteria. The action aforementioned peptides were studied on artificial membranes as well. The most active peptides resulted to be the short ones. Consequently, the minimal peptidic sequence necessary for the antibacterial activity was clearly determined: KYR. |
| doi_str_mv | 10.1016/j.peptides.2010.12.016 |
| format | Article |
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Hemoglobin is an animal protein described as a source of biologically active peptides. Peptic digestion of bovine hemoglobin alpha-chain allowed obtaining peptide fractions with antimicrobial activity. These peptides were purified by reverse-phase High-Performance Liquid Chromatography (HPLC) and characterized by mass spectrometry. The minimal inhibitory concentration and mode of action of these peptides were studied against five bacterial strains including
Escherichia coli and
Salmonella enteritidis as Gram-negative bacteria and
Listeria innocua, Micrococcus luteus and
Staphylococcus aureus as Gram-positive bacteria. The action aforementioned peptides were studied on artificial membranes as well. The most active peptides resulted to be the short ones. Consequently, the minimal peptidic sequence necessary for the antibacterial activity was clearly determined: KYR.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/j.peptides.2010.12.016</identifier><identifier>PMID: 21262306</identifier><identifier>CODEN: PPTDD5</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Animal protein ; Anti-Infective Agents - chemistry ; antibacterial properties ; Antimicrobial ; artificial membranes ; Bacteria ; Bacteria - drug effects ; Biological and medical sciences ; cattle ; Chromatography, High Pressure Liquid ; Digestion ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Gram-negative bacteria ; Gram-positive bacteria ; Hemoglobin ; Hemoglobins - chemistry ; Liposome ; Listeria innocua ; mass spectrometry ; mechanism of action ; Membranes, Artificial ; MIC ; Microbial Sensitivity Tests ; Micrococcus luteus ; Minimal sequence ; minimum inhibitory concentration ; Peptides ; Peptides - chemistry ; reversed-phase high performance liquid chromatography ; Salmonella ; Salmonella Enteritidis ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Staphylococcus aureus ; Strain ; Vertebrates: endocrinology</subject><ispartof>Peptides (New York, N.Y. : 1980), 2011-04, Vol.32 (4), p.633-638</ispartof><rights>2011 Elsevier Inc.</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2011 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c486t-3c39020dca583587a910d396f3af920e5f2d7f42efdf2747732577ada61f1fe3</citedby><cites>FETCH-LOGICAL-c486t-3c39020dca583587a910d396f3af920e5f2d7f42efdf2747732577ada61f1fe3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0196978111000283$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24020481$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21262306$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Catiau, Lucie</creatorcontrib><creatorcontrib>Traisnel, Johnatan</creatorcontrib><creatorcontrib>Delval-Dubois, Véronique</creatorcontrib><creatorcontrib>Chihib, Nour-Eddine</creatorcontrib><creatorcontrib>Guillochon, Didier</creatorcontrib><creatorcontrib>Nedjar-Arroume, Naïma</creatorcontrib><title>Minimal antimicrobial peptidic sequence from hemoglobin alpha-chain: KYR</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>► Peptides derived from α 107–141 were antibacterial whatever the bacterial species. ► The most active peptide is the shortest one: α 137–141. ► Shortest the sequence of the peptide is, lowest the MIC is. ► KYR sequence is the minimal antimicrobial sequence from the hemoglobin α-chain. ► These active peptides were able to interact with cellular membrane.
Hemoglobin is an animal protein described as a source of biologically active peptides. Peptic digestion of bovine hemoglobin alpha-chain allowed obtaining peptide fractions with antimicrobial activity. These peptides were purified by reverse-phase High-Performance Liquid Chromatography (HPLC) and characterized by mass spectrometry. The minimal inhibitory concentration and mode of action of these peptides were studied against five bacterial strains including
Escherichia coli and
Salmonella enteritidis as Gram-negative bacteria and
Listeria innocua, Micrococcus luteus and
Staphylococcus aureus as Gram-positive bacteria. The action aforementioned peptides were studied on artificial membranes as well. The most active peptides resulted to be the short ones. Consequently, the minimal peptidic sequence necessary for the antibacterial activity was clearly determined: KYR.</description><subject>Animal protein</subject><subject>Anti-Infective Agents - chemistry</subject><subject>antibacterial properties</subject><subject>Antimicrobial</subject><subject>artificial membranes</subject><subject>Bacteria</subject><subject>Bacteria - drug effects</subject><subject>Biological and medical sciences</subject><subject>cattle</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Digestion</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gram-negative bacteria</subject><subject>Gram-positive bacteria</subject><subject>Hemoglobin</subject><subject>Hemoglobins - chemistry</subject><subject>Liposome</subject><subject>Listeria innocua</subject><subject>mass spectrometry</subject><subject>mechanism of action</subject><subject>Membranes, Artificial</subject><subject>MIC</subject><subject>Microbial Sensitivity Tests</subject><subject>Micrococcus luteus</subject><subject>Minimal sequence</subject><subject>minimum inhibitory concentration</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>reversed-phase high performance liquid chromatography</subject><subject>Salmonella</subject><subject>Salmonella Enteritidis</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Staphylococcus aureus</subject><subject>Strain</subject><subject>Vertebrates: endocrinology</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUlvFDEQRq0IlAwhfyHpC4JLD97aC6dEERBEEBIkh5wsx0vGo95i9yDx76lWT-BGTpZLr8rl7yF0SvCaYCLeb9djGKfkQ1lTPBfpGsoHaEWUZHVDhH6BVphoUWupyBF6VcoWY8y5VofoiBIqKMNiha6-pT51tq1sP6UuuTzcJ7gtw5OrSnjchd6FKuahqzahGx5aQPrKtuPG1m5jU_-h-nr34zV6GW1bwsn-PEY3nz7eXF7V198_f7m8uK4dV2KqmWMaU-ydbRRrlLSaYM-0iMxGTXFoIvUychqij1RyKRltpLTeChJJDOwYvV3GjnmAzcpkulRcaFvbh2FXjBJacdYw9jzZQDBUCQ7ku_-SRApKCBdYASoWFIIqJYdoxgzx5d-GYDOLMVvzJMbMYgyhBsrQeLp_Y3ffBf-37ckEAG_2gC3OtjHb3qXyj-OQGlcEuLOFi3Yw9iEDc_sTXhJgF2uN54-fL0QADb9SyKa4NDv0KQc3GT-k57b9A7hgtyc</recordid><startdate>20110401</startdate><enddate>20110401</enddate><creator>Catiau, Lucie</creator><creator>Traisnel, Johnatan</creator><creator>Delval-Dubois, Véronique</creator><creator>Chihib, Nour-Eddine</creator><creator>Guillochon, Didier</creator><creator>Nedjar-Arroume, Naïma</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>FBQ</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>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>7X8</scope><scope>7T7</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20110401</creationdate><title>Minimal antimicrobial peptidic sequence from hemoglobin alpha-chain: KYR</title><author>Catiau, Lucie ; Traisnel, Johnatan ; Delval-Dubois, Véronique ; Chihib, Nour-Eddine ; Guillochon, Didier ; Nedjar-Arroume, Naïma</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c486t-3c39020dca583587a910d396f3af920e5f2d7f42efdf2747732577ada61f1fe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animal protein</topic><topic>Anti-Infective Agents - chemistry</topic><topic>antibacterial properties</topic><topic>Antimicrobial</topic><topic>artificial membranes</topic><topic>Bacteria</topic><topic>Bacteria - drug effects</topic><topic>Biological and medical sciences</topic><topic>cattle</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Digestion</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gram-negative bacteria</topic><topic>Gram-positive bacteria</topic><topic>Hemoglobin</topic><topic>Hemoglobins - chemistry</topic><topic>Liposome</topic><topic>Listeria innocua</topic><topic>mass spectrometry</topic><topic>mechanism of action</topic><topic>Membranes, Artificial</topic><topic>MIC</topic><topic>Microbial Sensitivity Tests</topic><topic>Micrococcus luteus</topic><topic>Minimal sequence</topic><topic>minimum inhibitory concentration</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>reversed-phase high performance liquid chromatography</topic><topic>Salmonella</topic><topic>Salmonella Enteritidis</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Staphylococcus aureus</topic><topic>Strain</topic><topic>Vertebrates: endocrinology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Catiau, Lucie</creatorcontrib><creatorcontrib>Traisnel, Johnatan</creatorcontrib><creatorcontrib>Delval-Dubois, Véronique</creatorcontrib><creatorcontrib>Chihib, Nour-Eddine</creatorcontrib><creatorcontrib>Guillochon, Didier</creatorcontrib><creatorcontrib>Nedjar-Arroume, Naïma</creatorcontrib><collection>AGRIS</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>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Catiau, Lucie</au><au>Traisnel, Johnatan</au><au>Delval-Dubois, Véronique</au><au>Chihib, Nour-Eddine</au><au>Guillochon, Didier</au><au>Nedjar-Arroume, Naïma</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Minimal antimicrobial peptidic sequence from hemoglobin alpha-chain: KYR</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>2011-04-01</date><risdate>2011</risdate><volume>32</volume><issue>4</issue><spage>633</spage><epage>638</epage><pages>633-638</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><coden>PPTDD5</coden><abstract>► Peptides derived from α 107–141 were antibacterial whatever the bacterial species. ► The most active peptide is the shortest one: α 137–141. ► Shortest the sequence of the peptide is, lowest the MIC is. ► KYR sequence is the minimal antimicrobial sequence from the hemoglobin α-chain. ► These active peptides were able to interact with cellular membrane.
Hemoglobin is an animal protein described as a source of biologically active peptides. Peptic digestion of bovine hemoglobin alpha-chain allowed obtaining peptide fractions with antimicrobial activity. These peptides were purified by reverse-phase High-Performance Liquid Chromatography (HPLC) and characterized by mass spectrometry. The minimal inhibitory concentration and mode of action of these peptides were studied against five bacterial strains including
Escherichia coli and
Salmonella enteritidis as Gram-negative bacteria and
Listeria innocua, Micrococcus luteus and
Staphylococcus aureus as Gram-positive bacteria. The action aforementioned peptides were studied on artificial membranes as well. The most active peptides resulted to be the short ones. Consequently, the minimal peptidic sequence necessary for the antibacterial activity was clearly determined: KYR.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>21262306</pmid><doi>10.1016/j.peptides.2010.12.016</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0196-9781 |
| ispartof | Peptides (New York, N.Y. : 1980), 2011-04, Vol.32 (4), p.633-638 |
| issn | 0196-9781 1873-5169 |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Animal protein Anti-Infective Agents - chemistry antibacterial properties Antimicrobial artificial membranes Bacteria Bacteria - drug effects Biological and medical sciences cattle Chromatography, High Pressure Liquid Digestion Escherichia coli Fundamental and applied biological sciences. Psychology Gram-negative bacteria Gram-positive bacteria Hemoglobin Hemoglobins - chemistry Liposome Listeria innocua mass spectrometry mechanism of action Membranes, Artificial MIC Microbial Sensitivity Tests Micrococcus luteus Minimal sequence minimum inhibitory concentration Peptides Peptides - chemistry reversed-phase high performance liquid chromatography Salmonella Salmonella Enteritidis Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Staphylococcus aureus Strain Vertebrates: endocrinology |
| title | Minimal antimicrobial peptidic sequence from hemoglobin alpha-chain: KYR |
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