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Default Mapping residue-specific contacts of polymyxin B with lipopolysaccharide by saturation transfer difference NMR: insights into outer-membrane disruption and endotoxin neutralization.

Mapping residue-specific contacts of polymyxin B with lipopolysaccharide by saturation transfer difference NMR: insights into outer-membrane disruption and endotoxin neutralization.

Mapping residue-specific contacts of polymyxin B with lipopolysaccharide by saturation transfer difference NMR: insights into outer-membrane disruption and endotoxin neutralization.

Biopolymers. 2011;96(3):273-87

Authors: Bhunia A, Bhattacharjya S

Abstract
High-resolution interactions studies of molecules with lipopolysaccharide (LPS) or endotoxin are important for health, diseases and environment. LPS is the major constituent of the outer layer of the outer membrane of the gram-negative bacteria. LPS provides an efficient barrier against permeation of variety of compounds including antibacterial agents and antimicrobial peptides. In the intensive care units, LPS is known for the fatal septic shock syndromes. Because of LPS toxicity, high affinity LPS sensors are sought-after for the assessment of the quality of water and pharmaceutical products. Therefore, elucidation of binding epitopes of LPS interacting molecules would be vital for the development of antimicrobial, antiendotoxic molecules. Polymyxin B (PMB), an antibacterial cyclic lipo-peptide, is well known for its LPS sequestering and neutralizing activities. Here, we have used saturation transfer difference (STD) NMR methods for characterizing interactions of PMB with LPS from E. coli 0111:B4 and P. aeruginosa. The dissociation constants of the LPS-PMB complexes were obtained from concentration dependent STD studies. Further a detailed epitope mapping of PMB has been carried out in E. coli 0111:B4 LPS micelles. Experiments including one-dimensional 1H STD, two-dimensional 1H-1H STD-TOCSY and naturalabundance 13C-1H STD-HSQC, are performed to determine the site(s) of interactions of PMB with endotoxin at atomic resolution. Our studies reveal that the hydrophobic sidechains of PMB including a part of the N-terminus lipidic tail demonstrate close contacts with LPS. In contrast, cyclic backbone structure of PMB has the lowest STD effects suggesting a rather loose association with endotoxin.


PMID: 20683937 [PubMed - indexed for MEDLINE]



Source: PubMed
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