Abstract：
:The aim of the study was to isolate and characterize novel antimicrobial peptides from peptide phage library with antimicrobial activity against multidrug resistant Listeria monocytogenes. Combinatorial phage-display library was used to affinity select peptides binding to the cell surface of multidrug resistant L. monocytogenes. After several rounds of affinity selection followed by sequencing, three peptides were revealed as the most promising candidates. Peptide L2 exhibited features common to antimicrobial peptides (AMPs), and was rich in Asp, His and Lys residues. Peptide L3 (NSWIQAPDTKSI), like peptide L2, inhibited bacterial growth in vitro, without any hemolytic or cytotoxic effects on eukaryotic cells. L1 peptide showed no inhibitory effect on Listeria. Structurally, peptides L2 and L3 formed random coils composed of α-helix and β-sheet units. Peptides L2 and L3 exhibited antimicrobial activity against multidrug resistant isolates of L. monocytogenes with no haemolytic or toxic effects. Both peptides identified in this study have the potential to be beneficial in human and veterinary medicine.
journal_name
Microbiol Resjournal_title
Microbiological researchauthors
Flachbartova Z,Pulzova L,Bencurova E,Potocnakova L,Comor L,Bednarikova Z,Bhide Mdoi
10.1016/j.micres.2016.04.010subject
Has Abstractpub_date
2016-07-01 00:00:00pages
34-41eissn
0944-5013issn
1618-0623pii
S0944-5013(16)30165-3journal_volume
188-189pub_type
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