{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Quintero D"],"funding":["NIGMS NIH HHS"],"pagination":["2079-2094"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6883771"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["28(12)"],"pubmed_abstract":["Sunflower trypsin inhibitor (SFTI) is a 14-amino-acid bicyclic peptide that contains a single internal disulfide bond. We initially constructed chimeras of SFTI with N-terminal secretion signals from the <i>Escherichia coli</i> OmpA and <i>Pseudomonas aeruginosa</i> ToxA, but only detected small amounts of protease inhibition resulting from these constructs. A substantially higher degree of protease inhibition was detected from a C-terminal SFTI fusion with <i>E. coli</i> YebF, which radiated more than a centimeter from an individual colony of <i>E. coli</i> using a culture-based inhibitor assay. Inhibitory activity was further improved in YebF-SFTI fusions by the addition of a trypsin cleavage signal immediately upstream of SFTI, and resulted in production of a 14-amino-acid, disulfide-bo"],"journal":["Journal of microbiology and biotechnology"],"pubmed_title":["Co-Expression of a Chimeric Protease Inhibitor Secreted by a Tumor-Targeted <i>Salmonella</i> Protects Therapeutic Proteins from Proteolytic Degradation."],"pmcid":["PMC6883771"],"funding_grant_id":["SC3 GM098207","R25 GM063787"],"pubmed_authors":["Vincent L","Quintero D","Carrafa J","Wohlschlegel J","Lee HJ","Bermudes D"],"additional_accession":[]},"is_claimable":false,"name":"Co-Expression of a Chimeric Protease Inhibitor Secreted by a Tumor-Targeted <i>Salmonella</i> Protects Therapeutic Proteins from Proteolytic Degradation.","description":"Sunflower trypsin inhibitor (SFTI) is a 14-amino-acid bicyclic peptide that contains a single internal disulfide bond. We initially constructed chimeras of SFTI with N-terminal secretion signals from the <i>Escherichia coli</i> OmpA and <i>Pseudomonas aeruginosa</i> ToxA, but only detected small amounts of protease inhibition resulting from these constructs. A substantially higher degree of protease inhibition was detected from a C-terminal SFTI fusion with <i>E. coli</i> YebF, which radiated more than a centimeter from an individual colony of <i>E. coli</i> using a culture-based inhibitor assay. Inhibitory activity was further improved in YebF-SFTI fusions by the addition of a trypsin cleavage signal immediately upstream of SFTI, and resulted in production of a 14-amino-acid, disulfide-bo","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Dec","modification":"2026-05-03T14:48:21.199Z","creation":"2020-10-29T12:19:41Z"},"accession":"S-EPMC6883771","cross_references":{"pubmed":["30661346"],"doi":["10.4014/jmb.1807.08036","10.4014/jmb.1808.08036"]}}