Bulky aromatic amino acids increase the antibacterial activity of 15-residue bovine lactoferricin derivatives.
J Pept Sci
; 7(8): 425-32, 2001 Aug.
Article
in En
| MEDLINE
| ID: mdl-11548058
ABSTRACT
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.
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Collection:
01-internacional
Health context:
3_ND
Database:
MEDLINE
Main subject:
Peptides
/
Amino Acids
/
Lactoferrin
/
Anti-Bacterial Agents
Limits:
Animals
Language:
En
Journal:
J Pept Sci
Year:
2001
Document type:
Article