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Using Siclopps for the Discovery of Novel Antimicrobial Peptides and Their Targets

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High throughput screening of SICLOPPS libraries afforded six distinct cyclic peptides that inhibit Escherichia coli growth both in liquid and solid media. One of these peptides (LN05) reduced both bacterial growth rate and caused cell aggregation in liquid media. Mutant bacteria immune to LN05 action were obtained at a frequency of 10-7. Overexpression of an E. coli genomic library in the presence of LN05 production resulted in enrichment of a single genomic construct, a fragment of the NarZ gene.
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Keywords: antimicrobial; cyclic peptides; functional complementation

Document Type: Review Article

Affiliations: Department of Biochemistry, the Albert Einstein College of Medicine, Bronx, NY 10461 USA;

Publication date: 2005-11-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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