{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T14:06:29Z","timestamp":1789135589350,"version":"build-2803163510"},"reference-count":55,"publisher":"American Chemical Society (ACS)","issue":"9","license":[{"start":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T00:00:00Z","timestamp":1786320000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T00:00:00Z","timestamp":1786320000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T00:00:00Z","timestamp":1786320000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100015691","name":"U.S. Department of Health and Human Services","doi-asserted-by":"publisher","award":["R42AI114114"],"award-info":[{"award-number":["R42AI114114"]}],"id":[{"id":"10.13039\/100015691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100015691","name":"U.S. Department of Health and Human Services","doi-asserted-by":"publisher","award":["R43AI165042"],"award-info":[{"award-number":["R43AI165042"]}],"id":[{"id":"10.13039\/100015691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,11]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Antisense oligomers show promise for the treatment of infectious diseases but face challenges as therapeutic agents due to limited uptake in bacteria. Although cell-penetrating peptides can serve as effective delivery vehicles, they may exhibit nonspecific effects and can contribute to resistance development. Aminoglycoside-peptide nucleic acid (PNA) conjugates represent a complementary delivery strategy that leverages the intrinsic cationic and membrane-interacting properties of aminoglycosides to enhance cellular uptake. In this work, we synthesized tobramycin-PNA (TOB-PNA) conjugates targeting the translation initiation region of the acyl carrier protein gene (acpP) in Enterobacterales. Conjugation of TOB to PNA enhanced target-binding stability, improved the inhibition of translation in vitro, and enhanced activity against Gram-negative bacteria. TOB-PNA activity was further enhanced in combination with the outer membrane-permeabilizing antibiotic polymyxin B (PMB), leading to improved antibacterial activity against clinically relevant Gram-negative pathogens, including drug-resistant isolates. Resistance studies demonstrated that the TOB-PNA conjugate, both alone and in combination with PMB, maintains antibacterial activity over prolonged exposure, suggesting a higher barrier to resistance evolution than conventional TOB treatment. Mammalian toxicity studies in HEK293T cells showed IC50 &amp;gt; 100 \u03bcM. Morphological analyses indicated that TOB-PNA treatment induces cellular stress and division abnormalities consistent with disruption of essential metabolic pathways, while PMB increased membrane permeability. In addition, TOB-PNA behaved synergistically with other compounds targeting distinct cellular processes, including fatty acid biosynthesis (triclosan), folate metabolism (trimethoprim), and cell morphology (A22).<\/jats:p>","DOI":"10.1021\/acsinfecdis.6c00322","type":"journal-article","created":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T13:02:08Z","timestamp":1786366928000},"page":"3144-3158","source":"Crossref","is-referenced-by-count":0,"title":["Tobramycin-Peptide Nucleic Acids Synergize with Polymyxin\nB and Other Bioactive Compounds to Inhibit Growth of Gram-Negative\nBacteria"],"prefix":"10.1021","volume":"12","author":[{"given":"Sandra","family":"Story","sequence":"first","affiliation":[{"name":"NUBAD, LLC , , ,","place":["Greenville, South Carolina, United States, 29605"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah","family":"Wicks","sequence":"additional","affiliation":[{"name":"NUBAD, LLC , , ,","place":["Greenville, South Carolina, United States, 29605"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sayantan","family":"Bhaduri","sequence":"additional","affiliation":[{"name":"NUBAD, LLC , , ,","place":["Greenville, South Carolina, United States, 29605"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alain S.","family":"Leutou","sequence":"additional","affiliation":[{"name":"NUBAD, LLC , , ,","place":["Greenville, South Carolina, United States, 29605"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5873-1066","authenticated-orcid":true,"given":"Dev P.","family":"Arya","sequence":"additional","affiliation":[{"name":"Clemson University , , , ,","place":["Clemson, South Carolina, United States, 29634"]},{"name":"NUBAD, LLC , , ,","place":["Greenville, South Carolina, United States, 29605"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,10]]},"reference":[{"issue":"7","key":"2026091109080841700_cit1","doi-asserted-by":"publisher","first-page":"939","DOI":"10.1097\/CCM.0000000000004371","article-title":"Key Takeaways\nFrom the U.S. CDC\u2019s 2019 Antibiotic Resistance Threats Report\nfor Frontline Providers","volume":"48","author":"Kadri","year":"2020","journal-title":"Crit. Care Med."},{"issue":"1","key":"2026091109080841700_cit2","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1086\/595011","article-title":"Bad bugs, no drugs: no ESKAPE! An update from the Infectious\nDiseases Society of America","volume":"48","author":"Boucher","year":"2009","journal-title":"Clin. Infect. Dis."},{"issue":"7586","key":"2026091109080841700_cit3","doi-asserted-by":"publisher","first-page":"336","DOI":"10.1038\/nature17042","article-title":"Antibacterial drug\ndiscovery in the resistance era","volume":"529","author":"Brown","year":"2016","journal-title":"Nature"},{"issue":"5","key":"2026091109080841700_cit4","doi-asserted-by":"publisher","first-page":"371","DOI":"10.1038\/nrd3975","article-title":"Platforms\nfor antibiotic discovery","volume":"12","author":"Lewis","year":"2013","journal-title":"Nat. Rev. Drug Discovery"},{"issue":"4","key":"2026091109080841700_cit5","doi-asserted-by":"publisher","DOI":"10.3390\/biomedicines9040416","article-title":"Silencing\nantibiotic resistance with\nantisense oligonucleotides","volume":"9","author":"Jani","year":"2021","journal-title":"Biomedicines"},{"key":"2026091109080841700_cit6","doi-asserted-by":"publisher","DOI":"10.1093\/femsre\/fuaf059","article-title":"Developing\nantisense oligomer biotics\n\u201casobiotics\u201d as precision antibacterials: designs, strategies,\nand considerations for future success","volume":"50","author":"Moustafa","year":"2025","journal-title":"FEMS\nMicrobiol. Rev."},{"key":"2026091109080841700_cit7","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1016\/j.trsl.2020.06.001","article-title":"Antisense\nantibacterial compounds","volume":"223","author":"Pifer","year":"2020","journal-title":"Transl. Res."},{"issue":"2","key":"2026091109080841700_cit8","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1089\/nat.2016.0656","article-title":"Molecular\nMechanisms of Antisense Oligonucleotides","volume":"27","author":"Crooke","year":"2017","journal-title":"Nucleic\nAcid Ther."},{"issue":"3","key":"2026091109080841700_cit9","doi-asserted-by":"publisher","first-page":"1055","DOI":"10.1007\/s00253-017-8671-0","article-title":"Advances in therapeutic bacterial antisense biotechnology","volume":"102","author":"Hegarty","year":"2018","journal-title":"Appl. Microbiol. Biotechnol."},{"issue":"6","key":"2026091109080841700_cit10","doi-asserted-by":"publisher","first-page":"1310","DOI":"10.1016\/0006-2952(94)90171-6","article-title":"Stability of peptide\nnucleic acids in human serum and cellular extracts","volume":"48","author":"Demidov","year":"1994","journal-title":"Biochem. Pharmacol."},{"issue":"4","key":"2026091109080841700_cit11","doi-asserted-by":"publisher","first-page":"360","DOI":"10.1038\/86753","article-title":"Bactericidal\nantisense effects of peptide-PNA conjugates","volume":"19","author":"Good","year":"2001","journal-title":"Nat. Biotechnol."},{"issue":"4","key":"2026091109080841700_cit12","doi-asserted-by":"publisher","first-page":"786","DOI":"10.1002\/cbdv.201000005","article-title":"Peptide\nnucleic acids (PNA) in chemical biology and drug discovery","volume":"7","author":"Nielsen","year":"2010","journal-title":"Chem. Biodivers"},{"issue":"3","key":"2026091109080841700_cit13","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijantimicag.2024.107083","article-title":"A systematic review of peptide nucleic\nacids (PNAs) with antibacterial activities: Efficacy, potential and\nchallenges","volume":"63","author":"El-Fateh","year":"2024","journal-title":"Int. J. Antimicrob. 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Sci."},{"issue":"8","key":"2026091109080841700_cit18","doi-asserted-by":"publisher","first-page":"4705","DOI":"10.1093\/nar\/gkab242","article-title":"Global RNA profiles show target selectivity\nand physiological effects of peptide-delivered antisense antibiotics","volume":"49","author":"Popella","year":"2021","journal-title":"Nucleic Acids Res."},{"issue":"4","key":"2026091109080841700_cit19","doi-asserted-by":"publisher","first-page":"1325","DOI":"10.1021\/bc070060v","article-title":"Pharmacokinetics,\nbiodistribution, stability and toxicity of a cell-penetrating peptide\u2013\nmorpholino oligomer conjugate","volume":"18","author":"Amantana","year":"2007","journal-title":"Bioconjugate\nChem."},{"issue":"7","key":"2026091109080841700_cit20","doi-asserted-by":"publisher","first-page":"1769","DOI":"10.1016\/j.bbamem.2007.03.029","article-title":"Peptide degradation\nis a critical determinant for cell-penetrating peptide uptake","volume":"1768","author":"Palm","year":"2007","journal-title":"Biochim. 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Lett."},{"issue":"1","key":"2026091109080841700_cit29","doi-asserted-by":"publisher","first-page":"160","DOI":"10.1021\/bc060249r","article-title":"Sequence-specific\ntargeting of RNA with an oligonucleotide-neomycin\nconjugate","volume":"18","author":"Charles","year":"2007","journal-title":"Bioconjugate Chem."},{"issue":"46","key":"2026091109080841700_cit30","doi-asserted-by":"publisher","DOI":"10.1002\/chem.202401674","article-title":"Advancing Nitrile-Aminothiol Strategy for Dual and\nSequential Bioconjugation","volume":"30","author":"Thombare","year":"2024","journal-title":"Chemistry"},{"issue":"3","key":"2026091109080841700_cit31","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1021\/acschembio.0c00822","article-title":"Uptake, stability, and activity of\nantisense anti-acpP PNA-peptide conjugates in Escherichia coli and the role of SbmA","volume":"16","author":"Yavari","year":"2021","journal-title":"ACS\nChem. Biol."},{"issue":"18","key":"2026091109080841700_cit32","doi-asserted-by":"publisher","first-page":"3094","DOI":"10.1016\/j.bmcl.2018.07.037","article-title":"Antimicrobial synergy\nbetween mRNA targeted peptide nucleic acid and antibiotics in Escherichia coli","volume":"28","author":"Castillo","year":"2018","journal-title":"Bioorg. Med.\nChem. Lett."},{"issue":"1","key":"2026091109080841700_cit33","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1093\/jac\/dki173","article-title":"Antimicrobial synergy\nbetween mRNA-\nand protein-level inhibitors","volume":"56","author":"Dryselius","year":"2005","journal-title":"J. Antimicrob.\nChemother."},{"issue":"3","key":"2026091109080841700_cit34","doi-asserted-by":"publisher","first-page":"971","DOI":"10.1021\/acsinfecdis.3c00645","article-title":"Understanding Antisense\nOligonucleotide Efficiency in Inhibiting Prokaryotic Gene Expression","volume":"10","author":"Story","year":"2024","journal-title":"ACS Infect. Dis."},{"issue":"1","key":"2026091109080841700_cit35","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1159\/000013861","article-title":"Aminoglycoside antibiotics","volume":"5","author":"Forge","year":"2000","journal-title":"Audiol.\nNeurotol."},{"issue":"4","key":"2026091109080841700_cit36","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1038\/nbt0498-355","article-title":"Antisense inhibition of gene expression in bacteria\nby PNA targeted to mRNA","volume":"16","author":"Good","year":"1998","journal-title":"Nat. Biotechnol."},{"key":"2026091109080841700_cit37","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2019.01032","article-title":"PNA length\nrestriction of antibacterial activity of peptide-PNA conjugates in Escherichia coli through effects of the inner membrane","volume":"10","author":"Goltermann","year":"2019","journal-title":"Front. Microbiol."},{"issue":"18","key":"2026091109080841700_cit38","doi-asserted-by":"publisher","first-page":"3094","DOI":"10.1016\/j.bmcl.2018.07.037","article-title":"Antimicrobial synergy\nbetween mRNA targeted peptide nucleic acid and antibiotics in E. coli","volume":"28","author":"Castillo","year":"2018","journal-title":"Bioorg. Med. Chem.\nLett."},{"key":"2026091109080841700_cit39","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2017.00687","article-title":"Exploration of using\nantisense peptide\nnucleic acid (PNA)-cell penetrating peptide (CPP) as a novel bactericide\nagainst fire blight pathogen Erwinia amylovora","volume":"8","author":"Patel","year":"2017","journal-title":"Front. Microbiol."},{"issue":"40","key":"2026091109080841700_cit40","doi-asserted-by":"publisher","first-page":"16169","DOI":"10.1073\/pnas.1311066110","article-title":"Bacterial cytological\nprofiling rapidly identifies the cellular pathways targeted by antibacterial\nmolecules","volume":"110","author":"Nonejuie","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"6","key":"2026091109080841700_cit41","doi-asserted-by":"publisher","first-page":"2421","DOI":"10.1128\/aem.63.6.2421-2431.1997","article-title":"Bacterial viability\nand antibiotic susceptibility testing with SYTOX green nucleic acid\nstain","volume":"63","author":"Roth","year":"1997","journal-title":"Appl. Environ. Microbiol."},{"issue":"8","key":"2026091109080841700_cit42","doi-asserted-by":"publisher","first-page":"1914","DOI":"10.1128\/AAC.40.8.1914","article-title":"Comparison of three\ndifferent in vitro methods of detecting synergy: time-kill, checkerboard,\nand E test","volume":"40","author":"White","year":"1996","journal-title":"Antimicrob. Agents Chemother."},{"issue":"3","key":"2026091109080841700_cit43","doi-asserted-by":"publisher","first-page":"345","DOI":"10.1016\/j.cll.2019.04.002","article-title":"E. J..\nWhen One Drug is Not Enough: Context, Methodology, and Future Prospects\nin Antibacterial Synergy Testing","volume":"39","author":"Krohn-Brennan","year":"2020","journal-title":"Clin. Lab\nMed."},{"issue":"12","key":"2026091109080841700_cit44","doi-asserted-by":"publisher","first-page":"4124","DOI":"10.1128\/JCM.01121-14","article-title":"When does\n2 plus 2 equal 5? A review of antimicrobial synergy testing","volume":"52","author":"Doern","year":"2014","journal-title":"J. Clin. Microbiol."},{"key":"2026091109080841700_cit45","volume-title":"Methods\nfor Determining\nBactericidal Activity of Antimicrobial Agents; Approved Guideline","author":"Barry","year":"1999"},{"issue":"6","key":"2026091109080841700_cit46","doi-asserted-by":"publisher","first-page":"2294","DOI":"10.1128\/JCM.39.6.2294-2297.2001","article-title":"Biofilm formation by gram-negative\nbacteria on central venous catheter connectors: effect of conditioning\nfilms in a laboratory model","volume":"39","author":"Murga","year":"2001","journal-title":"J. Clin. Microbiol."},{"issue":"3","key":"2026091109080841700_cit47","doi-asserted-by":"publisher","first-page":"629","DOI":"10.1128\/MMBR.00078-15","article-title":"Klebsiella pneumoniae: Going on the Offense with a Strong Defense","volume":"80","author":"Paczosa","year":"2016","journal-title":"Microbiol. Mol. Biol. 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Chem."},{"issue":"16","key":"2026091109080841700_cit51","doi-asserted-by":"publisher","first-page":"11110","DOI":"10.1074\/jbc.274.16.11110","article-title":"Mechanism of triclosan\ninhibition of bacterial fatty\nacid synthesis","volume":"274","author":"Heath","year":"1999","journal-title":"J. Biol. Chem."},{"issue":"1","key":"2026091109080841700_cit52","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1002\/j.1875-9114.1981.tb03548.x","article-title":"Trimethoprim: mechanisms of action,\nantimicrobial activity, bacterial resistance, pharmacokinetics, adverse\nreactions, and therapeutic indications","volume":"1","author":"Gleckman","year":"1981","journal-title":"Pharmacotherapy"},{"issue":"22","key":"2026091109080841700_cit53","doi-asserted-by":"publisher","first-page":"4852","DOI":"10.1021\/bi900014d","article-title":"A22 disrupts the bacterial actin\ncytoskeleton by directly binding and inducing a low-affinity state\nin MreB","volume":"48","author":"Bean","year":"2009","journal-title":"Biochemistry"},{"key":"2026091109080841700_cit54","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1016\/j.micpath.2016.07.007","article-title":"Antibacterial,\ncyto and genotoxic activities of A22\ncompound ((S-3, 4-dichlorobenzyl) isothiourea hydrochloride)","volume":"99","author":"Bonez","year":"2016","journal-title":"Microb. Pathog."},{"key":"2026091109080841700_cit55","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2025.1605813","article-title":"Synergistic\naction\nbetween peptide-neomycin conjugates and polymyxin B against multidrug-resistant\ngram-negative pathogens","volume":"16","author":"Story","year":"2025","journal-title":"Front. Microbiol."}],"container-title":["ACS Infectious Diseases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acsinfecdis.6c00322","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/aidcbc\/article-pdf\/12\/9\/3144\/66470750\/acsinfecdis.6c00322.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/aidcbc\/article-pdf\/12\/9\/3144\/66470750\/acsinfecdis.6c00322.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T13:11:51Z","timestamp":1789132311000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/aidcbc\/article\/12\/9\/3144\/5251072\/Tobramycin-Peptide-Nucleic-Acids-Synergize-with"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,10]]},"references-count":55,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2026,8,10]]},"published-print":{"date-parts":[[2026,9,11]]}},"URL":"https:\/\/doi.org\/10.1021\/acsinfecdis.6c00322","relation":{},"ISSN":["2373-8227"],"issn-type":[{"value":"2373-8227","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,10]]}}}