The Use of an Organo-Selenium Peptide to Develop New Antimicrobials That Target a Specific Bacteria.
Ontology highlight
ABSTRACT: This study examines the use of a covalently selenium-bonded peptide and phage that binds to the Yersinia pestis F1 antigen for the targeting and killing of E. coli expressing this surface antigen. Using a Ph.D.-12 phage-display library for affinity selection of the phage which would bind the F1 antigen of Y. pestis, a phage displaying a peptide that binds the F1 antigen with high affinity and specificity was identified. Selenium was then covalently attached to the display phage and the corresponding F1-antigen-binding peptide. Both the phage and peptides with selenium covalently attached retained their binding specificity for the Y. pestis F1 antigen. The phage or peptide not labeled with selenium did not kill the targeted bacteria, while the phage or peptide labeled with selenium did. In
SUBMITTER: Tran P
PROVIDER: S-EPMC8224008 | biostudies-literature | 2021 May
REPOSITORIES: biostudies-literature
ACCESS DATA