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Bulky aromatic amino acids increase the antibacterial activity of 15‐residue bovine lactoferricin derivatives
Author(s) -
Haug Bengt Erik,
Skar Merete L.,
Svendsen John S.
Publication year - 2001
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.338
Subject(s) - aromatic amino acids , residue (chemistry) , chemistry , peptide , amino acid , antibacterial activity , amino acid residue , escherichia coli , biochemistry , stereochemistry , peptide sequence , bacteria , biology , gene , genetics
A model peptide, FKCRRWQWRMKKLGA, residues 17–31 of bovine lactoferricin, has been subjected to structure–antibacterial activity relationship studies. The two Trp residues are very important for antibacterial activity, and analogue studies have demonstrated the significance of the size, shape and aromatic character of the side chains. In the current study we have replaced Trp residues in the model peptide with bulky aromatic amino acids to elucidate further the importance of size and shape. The counterproductive Cys residue in position 3 was also replaced by these aromatic amino acids. The largest aromatic amino acids employed resulted in the most active peptides. The peptides containing these hydrophobic residues were generally more active against Staphylococcus aureus than against Escherichia coli , indicating that the bacterial specificity as well as the antibacterial efficiency can be altered by employing large hydrophobic aromatic amino acid residues. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.