{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T19:36:51Z","timestamp":1790537811497,"version":"4.1.0"},"reference-count":56,"publisher":"American Chemical Society (ACS)","issue":"5","license":[{"start":{"date-parts":[[2020,3,5]],"date-time":"2020-03-05T00:00:00Z","timestamp":1583366400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2020,3,5]],"date-time":"2020-03-05T00:00:00Z","timestamp":1583366400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2020,3,5]],"date-time":"2020-03-05T00:00:00Z","timestamp":1583366400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/501100001459","name":"Ministry of Education - Singapore","doi-asserted-by":"publisher","award":["MOE2013-T3-1-002"],"award-info":[{"award-number":["MOE2013-T3-1-002"]}],"id":[{"id":"10.13039\/501100001459","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001381","name":"National Research Foundation Singapore","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001381","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020,5,8]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Antibiotic-resistant infections are predicted to kill 10 million people worldwide per year by 2050 and to cost the global economy 100 trillion USD. Novel approaches and alternatives to conventional antibiotics are urgently required to combat antimicrobial resistance. We have synthesized a chitosan-based oligolysine antimicrobial peptide, CSM5-K5 (where CSM denotes chitosan monomer repeat units and K denotes lysine amino acid repeat units), that targets multidrug-resistant (MDR) bacterial species. Here, we show that CSM5-K5 exhibits rapid bactericidal activity against methicillin-resistant Staphylococcus aureus (MRSA), MDR Escherichia coli, and vancomycin-resistant Enterococcus faecalis (VRE). Combinatorial therapy of CSM5-K5 with antibiotics to which each organism is otherwise resistant restores sensitivity to the conventional antibiotic. CSM5-K5 alone significantly reduced preformed bacterial biofilm by 2\u20134 orders of magnitude and, in combination with conventional antibiotics, reduced preformed biofilm by more than 2\u20133 orders of magnitude at subinhibitory concentrations. Moreover, using a mouse excisional wound infection model, CSM5-K5 treatment reduced bacterial burdens by 1\u20133 orders of magnitude and acted synergistically with oxacillin, vancomycin, and streptomycin to clear MRSA, VRE, and MDR E.\u00a0coli, respectively. Importantly, little to no resistance against CSM5-K5 arose for any of the three MDR bacteria during 15 days of serial passage. Furthermore, low level resistance to CSM5-K5 that did arise for MRSA conferred increased susceptibility (collateral sensitivity) to the \u03b2-lactam antibiotic oxacillin. This work demonstrates the feasibility and benefits of using this synthetic cationic peptide as an alternative to, or in combination with, traditional antibiotics to treat infections caused by MDR bacteria.<\/jats:p>","DOI":"10.1021\/acsinfecdis.0c00016","type":"journal-article","created":{"date-parts":[[2020,3,5]],"date-time":"2020-03-05T21:49:03Z","timestamp":1583444943000},"page":"1228-1237","source":"Crossref","is-referenced-by-count":72,"title":["Combined Efficacy of an Antimicrobial Cationic Peptide\nPolymer with Conventional Antibiotics to Combat Multidrug-Resistant\nPathogens"],"prefix":"10.1021","volume":"6","author":[{"given":"Kishore R. V.","family":"Thappeta","sequence":"first","affiliation":[{"name":"Nanyang Technological University , , 60 Nanyang Drive ,","place":["Singapore, 637551"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yogesh S.","family":"Vikhe","sequence":"additional","affiliation":[{"name":"Nanyang Technological University , ,","place":["Singapore, 637459"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adeline M. H.","family":"Yong","sequence":"additional","affiliation":[{"name":"Nanyang Technological University , , 60 Nanyang Drive ,","place":["Singapore, 637551"]},{"name":"Nanyang Technological University , , 60 Nanyang Drive ,","place":["Singapore, 637551"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3761-7517","authenticated-orcid":true,"given":"Mary B.","family":"Chan-Park","sequence":"additional","affiliation":[{"name":"Nanyang Technological University , ,","place":["Singapore, 637459"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5472-3074","authenticated-orcid":true,"given":"Kimberly A.","family":"Kline","sequence":"additional","affiliation":[{"name":"Nanyang Technological University , , 60 Nanyang Drive ,","place":["Singapore, 637551"]},{"name":"Nanyang Technological University , , 60 Nanyang Drive ,","place":["Singapore, 637551"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2020,3,5]]},"reference":[{"key":"2026081806131018400_cit1","volume-title":"Monitoring global progress on addressing\nantimicrobial resistance: analysis report of the second round of results\nof AMR country self-assessment survey 2018","author":"World Health Organization","year":"2018"},{"issue":"7","key":"2026081806131018400_cit2","doi-asserted-by":"publisher","first-page":"767","DOI":"10.1016\/S1473-3099(16)30127-X","article-title":"Reflecting\non the final report of the O\u2019Neill Review on Antimicrobial\nResistance","volume":"16","author":"Piddock","year":"2016","journal-title":"Lancet Infect. Dis."},{"issue":"7341","key":"2026081806131018400_cit3","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1038\/472032a","article-title":"Fix the antibiotics\npipeline","volume":"472","author":"Cooper","year":"2011","journal-title":"Nature"},{"key":"2026081806131018400_cit4","doi-asserted-by":"publisher","DOI":"10.1021\/acsinfecdis.9b00410","article-title":"Host Defense Peptide\nMimicking Peptide Polymer Exerting Fast, Broad Spectrum, and Potent\nActivities toward Clinically Isolated Multidrug-Resistant Bacteria","author":"Chen","year":"2020","journal-title":"ACS Infect. Dis."},{"issue":"11","key":"2026081806131018400_cit5","doi-asserted-by":"publisher","first-page":"1105","DOI":"10.1007\/s10118-019-2278-0","article-title":"Biofilm Disruption Utilizing \u03b1\/\u03b2 Chimeric\nPolypeptide Molecular Brushes","volume":"37","author":"Zhang","year":"2019","journal-title":"Chin. J. Polym.\nSci."},{"issue":"1","key":"2026081806131018400_cit6","doi-asserted-by":"publisher","first-page":"4792","DOI":"10.1038\/s41467-019-12702-8","article-title":"Enantiomeric\nglycosylated cationic block co-beta-peptides eradicate Staphylococcus\naureus biofilms and antibiotic-tolerant persisters","volume":"10","author":"Zhang","year":"2019","journal-title":"Nat. Commun."},{"issue":"3","key":"2026081806131018400_cit7","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1038\/nrmicro1098","article-title":"Antimicrobial peptides: pore formers or metabolic inhibitors\nin bacteria?","volume":"3","author":"Brogden","year":"2005","journal-title":"Nat. Rev. Microbiol."},{"issue":"6","key":"2026081806131018400_cit8","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0066440","article-title":"Activity determinants\nof helical antimicrobial peptides: a large-scale computational study","volume":"8","author":"He","year":"2013","journal-title":"PLoS One"},{"issue":"8","key":"2026081806131018400_cit9","doi-asserted-by":"publisher","first-page":"4635","DOI":"10.3390\/md12084635","article-title":"The effect of substituent,\ndegree of acetylation and positioning of the cationic charge on the\nantibacterial activity of quaternary chitosan derivatives","volume":"12","author":"Sahariah","year":"2014","journal-title":"Mar. Drugs"},{"issue":"2","key":"2026081806131018400_cit10","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1038\/nmat2915","article-title":"A polycationic antimicrobial and\nbiocompatible hydrogel with microbe membrane suctioning ability","volume":"10","author":"Li","year":"2011","journal-title":"Nat. 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Dis."},{"key":"2026081806131018400_cit28","volume-title":"Performance\nStandards for Antimicrobial Susceptibility Testing","author":"Clinical and Laboratory Standards\nInstitute","year":"2018","edition":"29"},{"issue":"136","key":"2026081806131018400_cit29","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1111\/apm.12099","article-title":"The role of bacterial\nbiofilms in chronic infections","volume":"121","author":"Bjarnsholt","year":"2013","journal-title":"APMIS Suppl"},{"issue":"8","key":"2026081806131018400_cit30","doi-asserted-by":"publisher","first-page":"3112","DOI":"10.1128\/AAC.48.8.3112-3118.2004","article-title":"Omiganan pentahydrochloride (MBI\n226), a topical 12-amino-acid cationic peptide: spectrum of antimicrobial\nactivity and measurements of bactericidal activity","volume":"48","author":"Sader","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"issue":"8","key":"2026081806131018400_cit31","doi-asserted-by":"publisher","first-page":"1680","DOI":"10.1016\/j.bbamem.2008.10.009","article-title":"Structure,\nmembrane orientation, mechanism, and function of pexiganan--a highly\npotent antimicrobial peptide designed from magainin","volume":"1788","author":"Gottler","year":"2009","journal-title":"Biochim. Biophys. Acta, Biomembr."},{"issue":"7061","key":"2026081806131018400_cit32","doi-asserted-by":"publisher","first-page":"975","DOI":"10.1038\/nature04051","article-title":"Plectasin\nis a peptide antibiotic with therapeutic potential from a saprophytic\nfungus","volume":"437","author":"Mygind","year":"2005","journal-title":"Nature"},{"issue":"7","key":"2026081806131018400_cit33","doi-asserted-by":"publisher","first-page":"3479","DOI":"10.1073\/pnas.75.7.3479","article-title":"Induced\ncell aggregation and mating in Streptococcus faecalis: evidence for\na bacterial sex pheromone","volume":"75","author":"Dunny","year":"1978","journal-title":"Proc. Natl. Acad.\nSci. U. S. A."},{"issue":"4","key":"2026081806131018400_cit34","doi-asserted-by":"publisher","first-page":"461","DOI":"10.3390\/antibiotics3040461","article-title":"Antimicrobial Peptide Resistance\nMechanisms of Gram-Positive Bacteria","volume":"3","author":"Nawrocki","year":"2014","journal-title":"Antibiotics\n(Basel, Switz.)"},{"issue":"1695","key":"2026081806131018400_cit35","doi-asserted-by":"publisher","first-page":"20150292","DOI":"10.1098\/rstb.2015.0292","article-title":"Bacterial strategies\nof resistance to antimicrobial peptides","volume":"371","author":"Joo","year":"2016","journal-title":"Philos.\nTrans. R. Soc., B"},{"issue":"1","key":"2026081806131018400_cit36","doi-asserted-by":"publisher","first-page":"VMBF-0006-2015","DOI":"10.1128\/microbiolspec.VMBF-0006-2015","article-title":"Bacterial Evasion of Host Antimicrobial Peptide Defenses","volume":"4","author":"Cole","year":"2016","journal-title":"Microbiol. 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Bacteriol."},{"key":"2026081806131018400_cit40","doi-asserted-by":"publisher","first-page":"24555","DOI":"10.3402\/iee.v4.24555","article-title":"Overview of ESBL-producing Enterobacteriaceae\nfrom a Nordic perspective","volume":"4","author":"Brolund","year":"2014","journal-title":"Infect Ecol Epidemiol"},{"issue":"3","key":"2026081806131018400_cit41","doi-asserted-by":"publisher","first-page":"422","DOI":"10.3390\/pathogens4030422","article-title":"Molecular Characterization\nof the Multidrug Resistant Escherichia coli ST131 Clone","volume":"4","author":"Schembri","year":"2015","journal-title":"Pathogens"},{"key":"2026081806131018400_cit42","doi-asserted-by":"publisher","first-page":"939","DOI":"10.2147\/DDDT.S107195","article-title":"Synergistic\neffects of antimicrobial peptide DP7 combined with antibiotics against\nmultidrug-resistant bacteria","volume":"11","author":"Wu","year":"2017","journal-title":"Drug Des., Dev.\nTher."},{"issue":"1","key":"2026081806131018400_cit43","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1093\/jac\/dkt322","article-title":"De novo generation of short antimicrobial\npeptides with enhanced stability and cell specificity","volume":"69","author":"Kim","year":"2014","journal-title":"J. Antimicrob. Chemother."},{"issue":"1","key":"2026081806131018400_cit44","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1517\/14712598.2013.844227","article-title":"Antimicrobial peptides: new drugs for bad bugs?","volume":"14","author":"Steckbeck","year":"2014","journal-title":"Expert Opin. Biol. Ther."},{"issue":"2","key":"2026081806131018400_cit45","doi-asserted-by":"publisher","first-page":"1329","DOI":"10.1128\/AAC.03937-14","article-title":"Engineered\ncationic antimicrobial peptides to overcome multidrug resistance by\nESKAPE pathogens","volume":"59","author":"Deslouches","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"issue":"12","key":"2026081806131018400_cit46","doi-asserted-by":"publisher","first-page":"1551","DOI":"10.1038\/nbt1267","article-title":"Antimicrobial and host-defense peptides as new anti-infective\ntherapeutic strategies","volume":"24","author":"Hancock","year":"2006","journal-title":"Nat. Biotechnol."},{"issue":"5615","key":"2026081806131018400_cit47","doi-asserted-by":"publisher","first-page":"2071","DOI":"10.1126\/science.1080613","article-title":"Role of mobile DNA in the evolution\nof vancomycin-resistant Enterococcus faecalis","volume":"299","author":"Paulsen","year":"2003","journal-title":"Science"},{"issue":"15","key":"2026081806131018400_cit48","doi-asserted-by":"publisher","first-page":"5977","DOI":"10.1073\/pnas.0600938103","article-title":"Identification of genes subject to positive selection\nin uropathogenic strains of Escherichia coli: a comparative genomics\napproach","volume":"103","author":"Chen","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. 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Med."},{"issue":"5","key":"2026081806131018400_cit51","doi-asserted-by":"publisher","first-page":"e00062-18","DOI":"10.1128\/mSystems.00062-18","article-title":"Comprehensive Functional Analysis of the Enterococcus\nfaecalis Core Genome Using an Ordered, Sequence-Defined Collection\nof Insertional Mutations in Strain OG1RF","volume":"3","author":"Dale","year":"2018","journal-title":"mSystems"},{"issue":"2","key":"2026081806131018400_cit52","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1038\/nprot.2007.521","article-title":"Agar and\nbroth dilution methods to determine the minimal inhibitory concentration\n(MIC) of antimicrobial substances","volume":"3","author":"Wiegand","year":"2008","journal-title":"Nat. Protoc."},{"issue":"3","key":"2026081806131018400_cit53","doi-asserted-by":"publisher","first-page":"290","DOI":"10.1016\/j.mayocp.2012.01.007","article-title":"Current concepts in laboratory testing to guide antimicrobial\ntherapy","volume":"87","author":"Jenkins","year":"2012","journal-title":"Mayo Clin. Proc."},{"issue":"2","key":"2026081806131018400_cit54","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1016\/S0021-9258(18)65573-5","article-title":"Antagonists\nof nucleic acid derivatives. VIII. Synergism in combinations of biochemically\nrelated antimetabolites","volume":"208","author":"Elion","year":"1954","journal-title":"J. Biol. Chem."},{"issue":"7535","key":"2026081806131018400_cit55","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1038\/nature14098","article-title":"A new antibiotic kills\npathogens without detectable resistance","volume":"517","author":"Ling","year":"2015","journal-title":"Nature"},{"issue":"12","key":"2026081806131018400_cit56","doi-asserted-by":"publisher","first-page":"1644","DOI":"10.1093\/infdis\/jix541","article-title":"Enterococcus faecalis Modulates Immune\nActivation and Slows Healing During Wound Infection","volume":"216","author":"Chong","year":"2017","journal-title":"J. Infect. 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