Work

Systematic mutagenesis of oncocin reveals enhanced activity and insights into the mechanisms of antimicrobial activity

Year: 2018

Type: article

Abstract: transcription / translation assay indicated that the increased activity was not because of stronger ribosome binding. Rather a cellular internalization assay revealed a higher internalization rate for the optimized analogs thereby suggesting a mechanism to increase potency. In addition, we found that the optimized peptides' benefit is dependent upon nutrient-depleted media conditions. The molecular design and characterization strategies have broad potential for development of antimicrobial peptides.

Source: Molecular Systems Design & Engineering

DOI: 10.1039/c8me00051d

Authors: Pin-Kuang Lai, Kathryn Geldart, Seth Ritter, Yiannis N. Kaznessis, Benjamin J. Hackel

Institution: University of Minnesota

Language: English

Topic: Antimicrobial Peptides and Activities

Subfield: Microbiology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: green

Funders: National Science Foundation, National Institutes of Health, National Institute of General Medical Sciences

Awards: Lactic Acid Bacteria that Detect & Inhibit Enterococci in the Mammalian GI Tract, Multiscale Models for Synthetic Biological Antibiotic Technologies, G458026666, Engineering Antimicrobial Polypeptides against Pathogenic Bacteria