{Reference Type}: Journal Article
{Title}: Design of a Novel Lysine Isopeptide 1018KI11 with Potent Antimicrobial Activity as a Safe and Stable Food Preservative Candidate.
{Author}: Wang Q;Yang Y;Dong X;Wang H;Ding L;Wang X;
{Journal}: J Agric Food Chem
{Volume}: 72
{Issue}: 14
{Year}: 2024 Apr 10
{Factor}: 5.895
{DOI}: 10.1021/acs.jafc.3c09484
{Abstract}: Antimicrobial peptides are potent food additive candidates, but most of them are sensitive to proteases, which limits their application. Therefore, we substituted arginine for lysine and introduced a lysine isopeptide bond to peptide IDR-1018 in order to improve its enzymatic stability. Subsequently, the protease stability and antimicrobial/antibiofilm activity of the novel peptides (1018K2-1018KI11) were investigated. The data revealed that the antienzymatic potential of 1018KI11 to bromelain and papain increased by 2-8 folds and 16 folds, respectively. The minimum inhibitory concentration (MIC) of 1018KI11 against methicillin-resistant Staphylococcus aureus (MRSA) ATCC43300 and Escherichia coli (E. coli) ATCC25922 was reduced 2-fold compared to 1018K11. Mechanism exploration suggested that 1018KI11 was more effective than 1018K11 in disrupting the cell barrier and damaging genomic DNA. Additionally, 1018KI11 at certain concentration conditions (2-64 μg/mL) reduced biofilm development of MRSA ATCC43300 by 4.9-85.9%. These data indicated that novel peptide 1018KI11 is a potential food preservative candidate.