Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain
Cationic antibacterial peptides are potentially therapeutic in the treatment of sepsis, because of their amalgamated antibacterial and lipopolysaccharide-binding activities. We prepared acyl analogues of the peptide fragment of human lactoferrin, which originally had weak antibacterial activity. It...
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| Veröffentlicht in: | Journal of antimicrobial chemotherapy 2003-05, Vol.51 (5), p.1159-1165 |
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| container_title | Journal of antimicrobial chemotherapy |
| container_volume | 51 |
| creator | Majerle, Andreja Kidrič, Jurka Jerala, Roman |
| description | Cationic antibacterial peptides are potentially therapeutic in the treatment of sepsis, because of their amalgamated antibacterial and lipopolysaccharide-binding activities. We prepared acyl analogues of the peptide fragment of human lactoferrin, which originally had weak antibacterial activity. It was found that 12 carbon units constitute the optimal acyl chain length, enhancing the antibacterial activity and binding of lipopolysaccharide by up to two orders of magnitude. Lactoferrin-based lipopeptides approached the activity of polymyxin B, a lipopeptide of natural origin, but were also active against Gram-positive bacteria. |
| doi_str_mv | 10.1093/jac/dkg219 |
| format | Article |
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We prepared acyl analogues of the peptide fragment of human lactoferrin, which originally had weak antibacterial activity. It was found that 12 carbon units constitute the optimal acyl chain length, enhancing the antibacterial activity and binding of lipopolysaccharide by up to two orders of magnitude. Lactoferrin-based lipopeptides approached the activity of polymyxin B, a lipopeptide of natural origin, but were also active against Gram-positive bacteria.</description><identifier>ISSN: 0305-7453</identifier><identifier>ISSN: 1460-2091</identifier><identifier>EISSN: 1460-2091</identifier><identifier>DOI: 10.1093/jac/dkg219</identifier><identifier>PMID: 12697647</identifier><identifier>CODEN: JACHDX</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Acylation ; Anti-Infective Agents - pharmacology ; Antibacterial agents ; antibacterial peptide ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Biological and medical sciences ; Chemical Phenomena ; Chemistry, Physical ; endotoxin ; Endotoxins - chemistry ; Endotoxins - metabolism ; Escherichia coli - drug effects ; Escherichia coli - growth & development ; human lactoferrin ; Humans ; lactoferrin ; Lactoferrin - chemistry ; Lactoferrin - pharmacology ; Lipid A - chemistry ; lipopeptide ; Lipopolysaccharides - chemistry ; Medical sciences ; Peptide Fragments - chemistry ; Peptide Fragments - pharmacology ; Pharmacology. Drug treatments ; polymyxin B ; Protein Binding ; Recombinant Proteins - chemistry ; Recombinant Proteins - pharmacology ; Staphylococcus aureus - drug effects ; Staphylococcus aureus - growth & development ; Structure-Activity Relationship</subject><ispartof>Journal of antimicrobial chemotherapy, 2003-05, Vol.51 (5), p.1159-1165</ispartof><rights>2003 INIST-CNRS</rights><rights>Copyright Oxford University Press(England) May 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c445t-2035d238b9a2e311103ce6c457d9de2e597547a009b4b06ff9a5013fbb87ee3b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14919427$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12697647$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Majerle, Andreja</creatorcontrib><creatorcontrib>Kidrič, Jurka</creatorcontrib><creatorcontrib>Jerala, Roman</creatorcontrib><title>Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain</title><title>Journal of antimicrobial chemotherapy</title><addtitle>J. Antimicrob. Chemother</addtitle><description>Cationic antibacterial peptides are potentially therapeutic in the treatment of sepsis, because of their amalgamated antibacterial and lipopolysaccharide-binding activities. We prepared acyl analogues of the peptide fragment of human lactoferrin, which originally had weak antibacterial activity. It was found that 12 carbon units constitute the optimal acyl chain length, enhancing the antibacterial activity and binding of lipopolysaccharide by up to two orders of magnitude. Lactoferrin-based lipopeptides approached the activity of polymyxin B, a lipopeptide of natural origin, but were also active against Gram-positive bacteria.</description><subject>Acylation</subject><subject>Anti-Infective Agents - pharmacology</subject><subject>Antibacterial agents</subject><subject>antibacterial peptide</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Biological and medical sciences</subject><subject>Chemical Phenomena</subject><subject>Chemistry, Physical</subject><subject>endotoxin</subject><subject>Endotoxins - chemistry</subject><subject>Endotoxins - metabolism</subject><subject>Escherichia coli - drug effects</subject><subject>Escherichia coli - growth & development</subject><subject>human lactoferrin</subject><subject>Humans</subject><subject>lactoferrin</subject><subject>Lactoferrin - chemistry</subject><subject>Lactoferrin - pharmacology</subject><subject>Lipid A - chemistry</subject><subject>lipopeptide</subject><subject>Lipopolysaccharides - chemistry</subject><subject>Medical sciences</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - pharmacology</subject><subject>Pharmacology. Drug treatments</subject><subject>polymyxin B</subject><subject>Protein Binding</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Staphylococcus aureus - drug effects</subject><subject>Staphylococcus aureus - growth & development</subject><subject>Structure-Activity Relationship</subject><issn>0305-7453</issn><issn>1460-2091</issn><issn>1460-2091</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0U2L1DAYB_AiijuuXvwAEgQ9CHWT5q05yro6LgPOQUG8hCR9OpPZNq1JK8538EObecEFL55Ckt_z5OVfFM8Jfkuwolc7466au01F1INiQZjAZYUVeVgsMMW8lIzTi-JJSjuMseCiflxckEooKZhcFL9vwtYEBz2ECQ0tMmHy1rgJojddnjWo8-MwDt0-Gee2JvoGkPWh8WGDsvM__eQhHUvRdu5NQF1eHlqI0Qc0wjgdKtpoNscj7B5NW0CmaXLdEI51bt-h3NqHp8Wj1nQJnp3Hy-Lrh5sv18ty9fnjp-t3q9Ixxqf8OsqbitZWmQooIQRTB8IxLhvVQAVcSc6kwVhZZrFoW2U4JrS1tpYA1NLL4vWp7xiHHzOkSfc-Oeg6E2CYk5a0YrWq2X8hqRWjTMgMX_4Dd8McQ36ErogUgvNaZfTmhFwcUorQ6jH63sS9JlgfktQ5SX1KMuMX546z7aG5p-foMnh1BiY50-UfDs6ne8cUUaw6uPLkfJrg1999E-90vrjkevntu1a36_X6dvler-gfZsy4LQ</recordid><startdate>20030501</startdate><enddate>20030501</enddate><creator>Majerle, Andreja</creator><creator>Kidrič, Jurka</creator><creator>Jerala, Roman</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</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>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7U7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>NAPCQ</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20030501</creationdate><title>Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain</title><author>Majerle, Andreja ; Kidrič, Jurka ; Jerala, Roman</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c445t-2035d238b9a2e311103ce6c457d9de2e597547a009b4b06ff9a5013fbb87ee3b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Acylation</topic><topic>Anti-Infective Agents - pharmacology</topic><topic>Antibacterial agents</topic><topic>antibacterial peptide</topic><topic>Antibiotics. 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Drug treatments</topic><topic>polymyxin B</topic><topic>Protein Binding</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Staphylococcus aureus - drug effects</topic><topic>Staphylococcus aureus - growth & development</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Majerle, Andreja</creatorcontrib><creatorcontrib>Kidrič, Jurka</creatorcontrib><creatorcontrib>Jerala, Roman</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of antimicrobial chemotherapy</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Majerle, Andreja</au><au>Kidrič, Jurka</au><au>Jerala, Roman</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain</atitle><jtitle>Journal of antimicrobial chemotherapy</jtitle><addtitle>J. Antimicrob. Chemother</addtitle><date>2003-05-01</date><risdate>2003</risdate><volume>51</volume><issue>5</issue><spage>1159</spage><epage>1165</epage><pages>1159-1165</pages><issn>0305-7453</issn><issn>1460-2091</issn><eissn>1460-2091</eissn><coden>JACHDX</coden><abstract>Cationic antibacterial peptides are potentially therapeutic in the treatment of sepsis, because of their amalgamated antibacterial and lipopolysaccharide-binding activities. We prepared acyl analogues of the peptide fragment of human lactoferrin, which originally had weak antibacterial activity. It was found that 12 carbon units constitute the optimal acyl chain length, enhancing the antibacterial activity and binding of lipopolysaccharide by up to two orders of magnitude. 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| subjects | Acylation Anti-Infective Agents - pharmacology Antibacterial agents antibacterial peptide Antibiotics. Antiinfectious agents. Antiparasitic agents Biological and medical sciences Chemical Phenomena Chemistry, Physical endotoxin Endotoxins - chemistry Endotoxins - metabolism Escherichia coli - drug effects Escherichia coli - growth & development human lactoferrin Humans lactoferrin Lactoferrin - chemistry Lactoferrin - pharmacology Lipid A - chemistry lipopeptide Lipopolysaccharides - chemistry Medical sciences Peptide Fragments - chemistry Peptide Fragments - pharmacology Pharmacology. Drug treatments polymyxin B Protein Binding Recombinant Proteins - chemistry Recombinant Proteins - pharmacology Staphylococcus aureus - drug effects Staphylococcus aureus - growth & development Structure-Activity Relationship |
| title | Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain |
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