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dc.contributor.authorUppu, D. S. S. M.
dc.contributor.authorKonai, M. M.
dc.contributor.authorBaul, U.
dc.contributor.authorSingh, P.
dc.contributor.authorSiersma, T. K.
dc.contributor.authorSamaddar, S.
dc.contributor.authorVemparala, S.
dc.contributor.authorHamoen, L. W.
dc.contributor.authorNarayana, Chandrabhas
dc.contributor.authorHaldar, Jayanta
dc.date.accessioned2017-01-24T09:11:14Z-
dc.date.available2017-01-24T09:11:14Z-
dc.date.issued2016
dc.identifier.citationUppu, Dssm; Konai, M. M.; Baul, U.; Singh, P.; Siersma, T. K.; Samaddar, S.; Vemparala, S.; Hamoen, L. W.; Narayana, C.; Haldar, J., Isosteric substitution in cationic-amphiphilic polymers reveals an important role for hydrogen bonding in bacterial membrane interactions. Chemical Science 2016, 7 (7), 4613-4623 http://dx.doi.org/10.1039/c6sc00615aen_US
dc.identifier.citationChemical Scienceen_US
dc.identifier.citation7en_US
dc.identifier.citation7en_US
dc.identifier.issn2041-6520
dc.identifier.urihttp://hdl.handle.net/10572/2300-
dc.descriptionOpen Accessen_US
dc.description.abstractBiomimetic antibacterial polymers, the functional mimics of antimicrobial peptides (AMPs), targeting the bacterial cell membrane have been developed to combat the problem of antibiotic resistance. Amphiphilicity, a balance of cationic charge and hydrophobicity, in these polymers has been shown to be pivotal for their selective interactions with anionic lipid membranes of bacteria instead of zwitterionic mammalian (human erythrocyte) membranes. However, it is unclear if and to what extent hydrogen bonding in amphiphilic antibacterial polymers contributes to this membrane binding specificity. To address this, we employ isosteric substitution of ester with amide moieties that differ in their potency for hydrogen bonding in the side chains of N-alkyl maleimide based amphiphilic polymers. Our studies reveal that amide polymer (AC3P) is a potent antibacterial agent with high membrane-disrupting properties compared to its ester counterpart (EC3P). To understand these differences we performed bio-physical experiments and molecular dynamics (MD) simulations which showed strong interactions of AC3P including hydrogen bonding with lipid head groups of bacterial model lipid bilayers, that are absent in EC3P, make them selective for bacterial membranes. Mechanistic investigations of these polymers in bacteria revealed specific membrane disruptive activity leading to the delocalization of cell division related proteins. This unprecedented and unique concept provides an understanding of bacterial membrane interactions highlighting the role of hydrogen bonding. Thus, these findings will have significant implications in efficient design of potent membrane-active agents.en_US
dc.description.uri2041-6539en_US
dc.description.urihttp://dx.doi.org/10.1039/c6sc00615aen_US
dc.language.isoEnglishen_US
dc.publisherRoyal Society of Chemistryen_US
dc.rights@Royal Society of Chemistry, 2016en_US
dc.subjectChemistryen_US
dc.subjectAntimicrobial Peptide Actionen_US
dc.subjectMolecular-Dynamicsen_US
dc.subjectForce-Fielden_US
dc.subjectPore Formationen_US
dc.subjectAntibacterialen_US
dc.subjectOligomersen_US
dc.subjectProteinsen_US
dc.subjectBindingen_US
dc.subjectAmideen_US
dc.subjectAciden_US
dc.titleIsosteric substitution in cationic-amphiphilic polymers reveals an important role for hydrogen bonding in bacterial membrane interactionsen_US
dc.typeArticleen_US
Appears in Collections:Research Articles (Chandrabhas N.)
Research Papers (Jayanta Haldar)

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