dc.contributor.authorBhattacharjya, Surajit
dc.date.accessioned2016-01-20T07:14:30Z
dc.date.available2016-01-20T07:14:30Z
dc.date.issued2015
dc.identifier.citationBhattacharjya, S. (2015). NMR Structures and Interactions of Antimicrobial Peptides with Lipopolysaccharide: Connecting Structures to Functions. Current Topics in Medicinal Chemistry, 16(1), 4-15.en_US
dc.identifier.issn1568-0266en_US
dc.identifier.urihttp://hdl.handle.net/10220/39719
dc.description.abstractAntimicrobial peptides (AMPs) establish the first line of host defense mechanism against invading microorganisms including bacteria, viruses, fungi and parasites. In recent years, emergence and spread of antibiotic resistance bacterial pathogens have dawn considerable interest in investigations of AMPs. The ability of AMPs to exert lethality against multiple drug-resistant (MDR) bacteria has incited promising avenues for antibiotic development. As a mode of action, most AMPs perturb the membrane organization of bacterial cells. The outer membrane lipopolysaccharide (LPS) of Gram-negative bacteria establishes a superior permeability barrier, in contrast to the peptidoglycan layer of Gram-positive bacteria. Due to LPS barrier, development of antibiotics for drug resistant Gram- negative bacteria are more complicated, with only fewer compounds in the pipeline. Recent studies have demonstrated that LPS actively regulate mode of action of AMPs on the lethality of Gram-negative bacteria. LPS, also known as endotoxin, is the primary agent for septic shock syndromes in intensive care unit killing over 120,000 people in the USA. Currently, anti-sepsis therapies are greatly lacking. Therefore, LPS has been considered as a target for the development of antimicrobial and antisepsis drugs. In recent and past few years, 3-D structures and interactions of a number of AMPs have been determined in complex with LPS micelles. These studies have generated molecular insights towards mode of action and synergistic activity of AMPs in the outer membrane. In this review, atomic resolution structures and interactions of potent AMPs with LPS are discussed providing novel insights of their mode of action.en_US
dc.description.sponsorshipMOE (Min. of Education, S’pore)en_US
dc.format.extent17 p.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesCurrent Topics in Medicinal Chemistryen_US
dc.rights© 2016 Bentham Science Publishers. This is the author created version of a work that has been peer reviewed and accepted for publication by Current Topics in Medicinal Chemistry, Bentham Science Publishers. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.2174/1568026615666150703121943].en_US
dc.subjectAntimicrbial peptidesen_US
dc.subjectLipopolysaccharide (LPS)
dc.subjectOuter membrane
dc.subjectNMR
dc.titleNMR Structures and Interactions of Antimicrobial Peptides with Lipopolysaccharide: Connecting Structures to Functionsen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.2174/1568026615666150703121943
dc.description.versionAccepted versionen_US


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