Abstract
The antibacterial activity of bovine lactoferricin-(17-31)-pentadecapeptide against Escherichia coli and Staphylococcus aureus is sensitive to substitution of the Trp residues, and synthetic peptides with phenylalanine and any of eight non-proteinogenic aromatic amino acids greatly affected antibiotic activity. Using simple size-related descriptors for the new amino acids it is possible to develop quantitative structure-activity relationships (QSARs) that can be used as tools in the search for more active peptides.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids, Aromatic / genetics
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Amino Acids, Aromatic / metabolism*
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Animals
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Anti-Bacterial Agents / chemistry*
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Anti-Bacterial Agents / pharmacology*
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Cattle
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Computer Simulation
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Drug Design
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Escherichia coli / drug effects
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Lactoferrin / analogs & derivatives*
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Lactoferrin / chemistry
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Lactoferrin / genetics
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Lactoferrin / pharmacology*
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Microbial Sensitivity Tests
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Peptides*
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Quantitative Structure-Activity Relationship
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Staphylococcus aureus / drug effects
Substances
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Amino Acids, Aromatic
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Anti-Bacterial Agents
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Peptides
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Lactoferrin