Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorSinha, Sheetalen
dc.contributor.authorZheng, Liangzhenen
dc.contributor.authorMu, Yuguangen
dc.contributor.authorNg, Wun Jernen
dc.contributor.authorBhattacharjya, Surajiten
dc.identifier.citationSinha, S., Zheng, L., Mu, Y., Ng, W. J., & Bhattacharjya, S. (2017). Structure and Interactions of A Host Defense Antimicrobial Peptide Thanatin in Lipopolysaccharide Micelles Reveal Mechanism of Bacterial Cell Agglutination. Scientific Reports, 7(1), 17795-.en
dc.description.abstractHost defense cationic Antimicrobial Peptides (AMPs) can kill microorganisms including bacteria, viruses and fungi using various modes of action. The negatively charged bacterial membranes serve as a key target for many AMPs. Bacterial cell death by membrane permeabilization has been well perceived. A number of cationic AMPs kill bacteria by cell agglutination which is a distinctly different mode of action compared to membrane pore formation. However, mechanism of cell agglutinating AMPs is poorly understood. The outer membrane lipopolysaccharide (LPS) or the cell-wall peptidoglycans are targeted by AMPs as a key step in agglutination process. Here, we report the first atomic-resolution structure of thanatin, a cell agglutinating AMP, in complex with LPS micelle by solution NMR. The structure of thanatin in complex with LPS, revealed four stranded antiparallel β-sheet in a ‘head-tail’ dimeric topology. By contrast, thanatin in free solution assumed an antiparallel β-hairpin conformation. Dimeric structure of thanatin displayed higher hydrophobicity and cationicity with sites of LPS interactions. MD simulations and biophysical interactions analyses provided mode of LPS recognition and perturbation of LPS micelle structures. Mechanistic insights of bacterial cell agglutination obtained in this study can be utilized to develop antibiotics of alternative mode of action.en
dc.description.sponsorshipMOE (Min. of Education, S’pore)en
dc.description.sponsorshipNMRC (Natl Medical Research Council, S’pore)en
dc.format.extent13 p.en
dc.relation.ispartofseriesScientific Reportsen
dc.rights© 2017 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. Te images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit
dc.subjectBacterial Cell Agglutinationen
dc.titleStructure and Interactions of A Host Defense Antimicrobial Peptide Thanatin in Lipopolysaccharide Micelles Reveal Mechanism of Bacterial Cell Agglutinationen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Civil and Environmental Engineeringen
dc.contributor.schoolSchool of Biological Sciencesen
dc.contributor.schoolInterdisciplinary Graduate School (IGS)en
dc.contributor.researchNanyang Environment and Water Research Instituteen
dc.description.versionPublished versionen
item.fulltextWith Fulltext-
Appears in Collections:CEE Journal Articles
IGS Journal Articles
NEWRI Journal Articles
SBS Journal Articles

Citations 50

Updated on Feb 25, 2021

Citations 50

Updated on Mar 1, 2021

Page view(s) 50

Updated on Mar 1, 2021

Download(s) 50

Updated on Mar 1, 2021

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.