Type

Journal Article

Authors

Colin Hill
Kiera Considine
Thérèse Deasy
Tanya Clifford
Maire Begley
Avelino Alvarez-Ordóñez

Subjects

Microbiology

Topics
amino acid sequence food borne pathogens listeria monocytogenes antibacterial activity structure activity relationship cronobacter sakazakii antimicrobial activity antimicrobial peptide

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide αs2-Casein f(183-207). (2013)

Abstract Template-based studies on antimicrobial peptide (AMP) derivatives obtained through manipulation of the amino acid sequence are helpful to identify properties or residues that are important for biological activity. The present study sheds light on the importance of specific amino acids of the milk-derived αs2-casein f(183-207) peptide to its antibacterial activity against the food-borne pathogens Listeria monocytogenes and Cronobacter sakazakii. Trimming of the peptide revealed that residues at the C-terminal end of the peptide are important for activity. Removal of the last 5 amino acids at the C-terminal end and replacement of the Arg at position 23 of the peptide sequence by an Ala residue significantly decreased activity. These findings suggest that Arg23 is very important for optimal activity of the peptide. Substitution of the also positively charged Lys residues at positions 15 and 17 of the αs2-casein f(183-207) peptide also caused a significant reduction of the effectiveness against C. sakazakii, which points toward the importance of the positive charge of the peptide for its biological activity. Indeed, simultaneous replacement of various positively charged amino acids was linked to a loss of bactericidal activity. On the other hand, replacement of Pro residues at positions 14 and 20 resulted in a significantly increased antibacterial potency, and hydrophobic end tagging of αs2-casein f(193-203) and αs2-casein f(197-207) peptides with multiple Trp or Phe residues significantly increased their potency against L. monocytogenes. Finally, the effect of pH (4.5 to 7.4), temperature (4°C to 37°C), and addition of sodium and calcium salts (1% to 3%) on the activity of the 15-amino-acid αs2-casein f(193-207) peptide was also determined, and its biological activity was shown to be completely abolished in high-saline environments.
Collections Ireland -> University College Cork -> PubMed

Full list of authors on original publication

Colin Hill, Kiera Considine, Thérèse Deasy, Tanya Clifford, Maire Begley, Avelino Alvarez-Ordóñez

Experts in our system

1
Colin Hill
University College Cork
Total Publications: 351
 
2
Kiera Considine
University College Cork
 
3
Thérèse Deasy
University College Cork
Total Publications: 4
 
4
Tanya Clifford
University College Cork
Total Publications: 4
 
5
Maire Begley
University College Cork
Total Publications: 27
 
6
Avelino Alvarez-Ordóñez
University College Cork
Total Publications: 6