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dc.contributor.authorSinha, Sheetalen_US
dc.contributor.authorNg, Wun Jernen_US
dc.contributor.authorBhattacharjya, Surajiten_US
dc.identifier.citationSinha, S., Ng, W. J., & Bhattacharjya, S. (2020). NMR structure and localization of the host defense antimicrobial peptide thanatin in zwitterionic dodecylphosphocholine micelle : implications in antimicrobial activity. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1862(11), 183432-. doi:10.1016/j.bbamem.2020.183432en_US
dc.description.abstractAntimicrobial peptides (AMPs) are potentially vital as the next generation of antibiotics against multidrug resistant bacterial pathogens. Thanatin, an insect derived pathogen inducible 21-residue long antimicrobial peptide, demonstrates antimicrobial activity toward broad range of pathogens. Thanatin is an excellent candidate for antibiotics development due to potent in vivo activity in animal model and low toxicity to human cells. Recent studies indicated mode of action of thanatin could be intriguing and may comprise bacterial membrane permeabilization and interactions with periplasmic proteins. In order to better understand selectivity and membrane disruption, here, we determined 3-D structure of the thanatin in zwitterionic DPC-d38 micelle by NMR spectroscopy. The depth of insertion of thanatin into micelle structure was investigated by spin labelled doxyl lipids, 5-DSA and 16-DSA. DPC-bound structure of thanatin is defined by a -hairpin structure and an extended and turn conformations, for residues G1-I8, at the N-terminus. The -hairpin structure is delineated by two antiparallel -strands, residues I9-C11 and residues K17-R20, which is connected by loop consisted of residues N12-G16. There are cross -strands sidechain-sidechain packing interactions among hydrophobic and aromatic residues. Spin labelled lipid studies revealed a set of spatially proximal residues V6, I8, Q19, R20 and M21 may be deeply inserted into the hydrophobic core of the DPC micelle. Whilst, residues including those at the turn/loop are merely surface localized. The atomic resolution structure and orientation of thanatin in zwitterionic DPC micelle may be utilized for understating mode of action in lipid membrane and further development of non-toxic analogs.en_US
dc.description.sponsorshipMinistry of Education (MOE)en_US
dc.relation.ispartofBiochimica et Biophysica Acta (BBA) - Biomembranesen_US
dc.rights© 2020 Elsevier B.V. All rights reserved. This paper was published in Biochimica et Biophysica Acta (BBA) - Biomembranes and is made available with permission of Elsevier B.V.en_US
dc.subjectScience::Biological sciencesen_US
dc.titleNMR structure and localization of the host defense antimicrobial peptide thanatin in zwitterionic dodecylphosphocholine micelle : implications in antimicrobial activityen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.contributor.schoolInterdisciplinary Graduate School (IGS)en_US
dc.contributor.researchNanyang Environment and Water Research Instituteen_US
dc.description.versionAccepted versionen_US
dc.subject.keywordsAntimicrobial Peptidesen_US
dc.subject.keywordsHost Defense Antimicrobial Peptideen_US
dc.description.acknowledgementThis work has been supported by the research grant ARC18/13 from the Ministry of Education (MOE), Singapore. The pdb coordinates of the DPC bound structure of thanatin are deposited to RCSB Protein Data Bank with accession number 6AAB. NMR chemical shifts are deposited to BMRB database with accession code 36201.en_US
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