Related ArticlesNMR Structures and Interactions of Antimicrobial Peptides with Lipopolysaccharide: Connecting Structures to Functions.
Curr Top Med Chem. 2016;16(1):4-15
Authors: Bhattacharjya S
Abstract
Antimicrobial 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.
[NMR paper] NMR structure and binding of esculentin-1a (1-21)NH2 and its diastereomer to lipopolysaccharide: Correlation with biological functions.
NMR structure and binding of esculentin-1a (1-21)NH2 and its diastereomer to lipopolysaccharide: Correlation with biological functions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure and binding of esculentin-1a (1-21)NH2 and its diastereomer to lipopolysaccharide: Correlation with biological functions.
Biochim Biophys Acta. 2016 Apr;1858(4):800-12
Authors: Ghosh A, Bera S, Shai Y, Mangoni ML, Bhunia A
Abstract
The frog...
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06-18-2016 04:39 PM
[NMR paper] (19)F-NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids.
(19)F-NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids.
(19)F-NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids.
Biochim Biophys Acta. 2014 Mar 31;
Authors: Afonin S, Glaser RW, Sachse C, Salgado J, Wadhwani P, Ulrich AS
Abstract
Many amphiphilic antimicrobial peptides permeabilize bacterial membranes via successive steps of binding, re-alignment and/or oligomerization. Here, we have systematically...
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04-06-2014 02:01 AM
[NMR paper] Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures.
Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures.
Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures.
J Am Chem Soc. 2014 Jan 6;
Authors: Mao B, Tejero R, Baker D, Montelione GT
Abstract
We have found that refinement of protein NMR structures using Rosetta with experimental NMR restraints yields more accurate protein NMR structures than those that have been deposited in the PDB using standard refinement...
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01-08-2014 11:23 AM
The Chemoselective Reactions of Tyrosine-Containing G-Protein-Coupled Receptor Peptides with [Cp*Rh(H2O)3](OTf)2, Including 2D NMR Structures and the Biological Consequences
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H. Bauke Albada, Florian Wieberneit, Ingrid Dijkgraaf, Jessica H. Harvey, Jennifer L. Whistler, Raphael Stoll, Nils Metzler-Nolte and Richard H. Fish
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja303010k/aop/images/medium/ja-2012-03010k_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja303010k
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...
NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.
NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.
NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.
Biophys J. 2010 Oct 20;99(8):2507-15
Authors: Georgescu J, Munhoz VH, Bechinger B
The LAH4 family of histidine-rich peptides exhibits potent antimicrobial and DNA transfection activities, both of which require interactions...
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02-02-2011 02:40 AM
[NMR paper] NMR structures of anti-HIV D-peptides derived from the N-terminus of viral chemokine vMIP-II.
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Biochem Biophys Res Commun. 2005 Sep 30;335(3):651-8
Authors: Mori M, Liu D, Kumar S, Huang Z
The viral macrophage inflammatory protein-II (vMIP-II) encoded by Kaposi's sarcoma-associated herpesvirus has unique biological activities in that it blocks the cell entry by several different human immunodeficiency virus type 1 (HIV-1) strains via...
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12-01-2010 06:56 PM
[NMR paper] Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?
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Proteins. 2005 Jul 1;60(1):139-47
Authors: Garbuzynskiy SO, Melnik BS, Lobanov MY, Finkelstein AV, Galzitskaya OV
We have compared structures of 78 proteins determined by both NMR and X-ray methods. It is shown that X-ray and NMR structures...
NMR Structures and Interactions of Antimicrobial Peptides with Lipopolysaccharide: Connecting Structures to Functions.
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