Simple parameterization of non-proteinogenic amino acids for QSAR of antibacterial peptides

J Pept Sci. 2002 Jul;8(7):302-6. doi: 10.1002/psc.403.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids, Aromatic / genetics
  • Amino Acids, Aromatic / metabolism*
  • Animals
  • Anti-Bacterial Agents / chemistry*
  • Anti-Bacterial Agents / pharmacology*
  • Cattle
  • Computer Simulation
  • Drug Design
  • Escherichia coli / drug effects
  • Lactoferrin / analogs & derivatives*
  • Lactoferrin / chemistry
  • Lactoferrin / genetics
  • Lactoferrin / pharmacology*
  • Microbial Sensitivity Tests
  • Peptides*
  • Quantitative Structure-Activity Relationship
  • Staphylococcus aureus / drug effects

Substances

  • Amino Acids, Aromatic
  • Anti-Bacterial Agents
  • Peptides
  • Lactoferrin