{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["McGrath DM"],"funding":["NCI NIH HHS"],"pagination":["3477-82"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3587187"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["110(9)"],"pubmed_abstract":["Development of therapy against infections caused by antibiotic-resistant pathogens is a major unmet need in contemporary medicine. In previous work, our group chemically modified an antimicrobial peptidomimetic motif for targeted applications against cancer and obesity. Here, we show that the modified motif per se is resistant to proteolytic degradation and is a candidate antiinfective agent. We also show that the susceptibility of microorganisms to the drug is independent of bacterial growth phase. Moreover, this peptidomimetic selectively interferes with the integrity and function of the microbial surface lipid bilayer, data indicative that bacterial death results from membrane disruption followed by dissipation of membrane potential. Finally, we demonstrate two potential translational a"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Mechanism of action and initial evaluation of a membrane active all-D-enantiomer antimicrobial peptidomimetic."],"pmcid":["PMC3587187"],"funding_grant_id":["P30 CA016672"],"pubmed_authors":["Tarrand JJ","McGrath DM","Lasco TM","Kontoyiannis DP","Arap W","Driessen WH","Okhuysen PC","Sidman RL","Barbu EM","Pasqualini R"],"additional_accession":[]},"is_claimable":false,"name":"Mechanism of action and initial evaluation of a membrane active all-D-enantiomer antimicrobial peptidomimetic.","description":"Development of therapy against infections caused by antibiotic-resistant pathogens is a major unmet need in contemporary medicine. In previous work, our group chemically modified an antimicrobial peptidomimetic motif for targeted applications against cancer and obesity. Here, we show that the modified motif per se is resistant to proteolytic degradation and is a candidate antiinfective agent. We also show that the susceptibility of microorganisms to the drug is independent of bacterial growth phase. Moreover, this peptidomimetic selectively interferes with the integrity and function of the microbial surface lipid bilayer, data indicative that bacterial death results from membrane disruption followed by dissipation of membrane potential. Finally, we demonstrate two potential translational a","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Feb","modification":"2025-04-04T10:36:04.941Z","creation":"2019-03-27T01:05:32Z"},"accession":"S-EPMC3587187","cross_references":{"pubmed":["23345420"],"doi":["10.1073/pnas.1221924110"]}}