RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/32787108http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32787108http://www.w3.org/2000/01/rdf-schema#comment"Proline-rich antimicrobial peptides (PrAMPs) are promising lead compounds for developing new antimicrobials; however, their narrow spectrum of action is limiting. PrAMPs kill bacteria binding to their ribosomes and inhibiting protein synthesis. In this study, 133 derivatives of the PrAMP Bac7(1-16) were synthesized to identify the crucial residues for ribosome inactivation and antimicrobial activity. Then, five new Bac7(1-16) derivatives were conceived and characterized by antibacterial and membrane permeabilization assays, X-ray crystallography, and molecular dynamics simulations. Some derivatives displayed broad spectrum activity, encompassing Escherichia coli, Klebsiella pneumoniae, Acinetobacter baumanii, Pseudomonas aeruginosa, and Staphylococcus aureus. Two peptides out of five acquired a weak membrane-perturbing activity while maintaining the ability to inhibit protein synthesis. These derivatives became independent of the SbmA transporter, commonly used by native PrAMPs, suggesting that they obtained a novel route to enter bacterial cells. PrAMP-derived compounds could become new-generation antimicrobials to combat antibiotic-resistant pathogens."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.org/dc/terms/identifier"doi:10.1021/acs.jmedchem.0c00665"xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Beckert B."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Wilson D.N."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Mardirossian M."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Scocchi M."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Polikanov Y.S."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Valencic E."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Hilpert K."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Armas F."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Magistrato A."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Borisek J."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Buchmann J."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Sola R."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Syroegin E.A."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Collis D.W.P."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/author"Di Stasi A."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/name"J Med Chem"xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/pages"9590-9602"xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/title"Peptide Inhibitors of Bacterial Protein Synthesis with Broad Spectrum and SbmA-Independent Bactericidal Activity against Clinical Pathogens."xsd:string
http://purl.uniprot.org/citations/32787108http://purl.uniprot.org/core/volume"63"xsd:string
http://purl.uniprot.org/citations/32787108http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32787108
http://purl.uniprot.org/citations/32787108http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/32787108