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Unlocking NuriPep 1653 From Common Pea Protein: A Potent Antimicrobial Peptide to Tackle a Pan-Drug Resistant Acinetobacter baumannii.

Front Microbiol. 2019; 
Mohan NM,, Zorgani A, Jalowicki G, Kerr A, Khaldi N, Martins M.
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Peptide Synthesis … The peptide sequence was synthesized by GenScript (Piscataway, NJ, United States) using solid-phase 9-fluorenylmethoxycarbonyl (Fmoc) chemistry and purified to a purity of 95–99% using reverse-phase high-performance liquid chromatography (HPLC) … Get A Quote

摘要

While the antibiotic era has come and gone, antimicrobial peptides (AMPs) hold promise as novel therapies to treat multidrug resistant (MDR) pathogens in an age where the threat of multidrug resistance escalates worldwide. Here, we report the bactericidal properties of NuriPep 1653, a novel 22 mer and non-modified peptide. NuriPep 1653 was identified within the sequence of the non-antimicrobial P54 protein, which is involved in nutrient reservoir activity in Pisum sativum. Total bacterial clearance of Acinetobacter baumannii cells (1 × 108 cells/mL) was observed using only 4 × MIC (48 μg/mL) of NuriPep 1653 after just 20 min of treatment. We uncovered a synergistic interaction between NuriPep 1653 and anothe... More

关键词

Acinetobacter baumannii; antimicrobial peptides; data mining; hydrolyzed proteins; multidrug resistance; novel antimicrobials