Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/164026
Title: NMR structure and localization of the host defense peptide thanatinM21F in zwitterionic dodecylphosphocholine micelle: implications in antimicrobial and hemolytic activity
Authors: Sinha, Sheetal
Bhattacharjya, Surajit
Keywords: Science::Biological sciences
Issue Date: 2022
Source: Sinha, S. & Bhattacharjya, S. (2022). NMR structure and localization of the host defense peptide thanatinM21F in zwitterionic dodecylphosphocholine micelle: implications in antimicrobial and hemolytic activity. Journal of Membrane Biology, 255(2-3), 151-160. https://dx.doi.org/10.1007/s00232-022-00223-3
Journal: Journal of Membrane Biology
Abstract: Non-hemolytic antimicrobial peptides (AMPs) are vital lead molecules for the designing and development of peptide-based antibiotics. Thanatin a 21-amino acid long single disulfide bonded AMP is known to be highly non-hemolytic with a limited toxicity to human cells and model animals. Thanatin demonstrates a potent antibacterial activity against multidrug-resistant Gram-negative pathogens. A single mutated variant of thanatin replaced last residue Met21 to Phe or thanatin M21F has recently been found to be more active compared to the native peptide. In order to gain mechanistic insights toward bacterial cell lysis versus non-hemolysis, here, we report atomic resolution structure and mode insertion of thanatinM21F reconstituted into zwitterionic detergent micelle by use of solution NMR spectroscopy. The 3D structure of thanatinM21F in DPC micelle is defined by an anti-parallel β-sheet between residues I9-F21 with a central cationic loop, residues N12-R14. PRE NMR studies revealed hydrophobic core residues of thanatinM21F are deeply inserted in the DPC micelle, while residues at the extended N-terminal half of the peptide are appeared to be mostly surface localized. Marked structural differences of thanatin and thanatinM21F in negatively charged LPS and DPC micelle could be correlated with non-hemolytic and antibacterial activity.
URI: https://hdl.handle.net/10356/164026
ISSN: 0022-2631
DOI: 10.1007/s00232-022-00223-3
Rights: © 2022 The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
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