Literature DB >> 19180607

Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy.

Anirban Bhunia1, Ayyalusamy Ramamoorthy, Surajit Bhattacharjya.   

Abstract

Essential understanding: Elucidation of structural requirements and interactions of antimicrobial peptides with lipopolysaccharide (LPS) are essential to understand the mechanism of action of antimicrobial peptides. The highly active antimicrobial peptide MSI-594 (see figure for electrostatic potential surface) acquires a novel helical hairpin structure in complex with LPS. The structure and interactions of MSI-594 with LPS presented here provide important insights into the mechanism of outer membrane permeabilization by antimicrobial peptides.

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Year:  2009        PMID： 19180607     DOI： 10.1002/chem.200802635

Source DB:  PubMed          Journal:  Chemistry        ISSN： 0947-6539            Impact factor:   5.236


  37 in total

Review 1.  Cationic amphiphiles, a new generation of antimicrobials inspired by the natural antimicrobial peptide scaffold.

Authors:  Brandon Findlay; George G Zhanel; Frank Schweizer
Journal:  Antimicrob Agents Chemother       Date:  2010-08-09       Impact factor: 5.191

2.  Cell-wall interactions and the selective bacteriostatic activity of a miniature oligo-acyl-lysyl.

Authors:  Raquel F Epand; Hadar Sarig; Amram Mor; Richard M Epand
Journal:  Biophys J       Date:  2009-10-21       Impact factor: 4.033

Review 3.  Antimicrobial peptide resistance in Neisseria meningitidis.

Authors:  Yih-Ling Tzeng; David S Stephens
Journal:  Biochim Biophys Acta       Date:  2015-05-19

4.  Accelerated molecular dynamics simulation analysis of MSI-594 in a lipid bilayer.

Authors:  Shruti Mukherjee; Rajiv K Kar; Ravi Prakash Reddy Nanga; Kamal H Mroue; Ayyalusamy Ramamoorthy; Anirban Bhunia
Journal:  Phys Chem Chem Phys       Date:  2017-07-26       Impact factor: 3.676

Review 5.  Snake venoms: attractive antimicrobial proteinaceous compounds for therapeutic purposes.

Authors:  Nelson Gomes de Oliveira Junior; Marlon Henrique e Silva Cardoso; Octavio Luiz Franco
Journal:  Cell Mol Life Sci       Date:  2013-05-09       Impact factor: 9.261

6.  Disulfide-stabilized helical hairpin structure and activity of a novel antifungal peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli).

Authors:  Svetlana B Nolde; Alexander A Vassilevski; Eugene A Rogozhin; Nikolay A Barinov; Tamara A Balashova; Olga V Samsonova; Yuri V Baranov; Alexey V Feofanov; Tsezi A Egorov; Alexander S Arseniev; Eugene V Grishin
Journal:  J Biol Chem       Date:  2011-05-11       Impact factor: 5.157

7.  Resurrecting inactive antimicrobial peptides from the lipopolysaccharide trap.

Authors:  Harini Mohanram; Surajit Bhattacharjya
Journal:  Antimicrob Agents Chemother       Date:  2014-01-13       Impact factor: 5.191

8.  NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: mechanism of outer membrane permeabilization.

Authors:  Anirban Bhunia; Prerna N Domadia; Jaume Torres; Kevin J Hallock; Ayyalusamy Ramamoorthy; Surajit Bhattacharjya
Journal:  J Biol Chem       Date:  2009-12-03       Impact factor: 5.157

9.  Does cholesterol suppress the antimicrobial peptide induced disruption of lipid raft containing membranes?

Authors:  Austin J McHenry; Michele F M Sciacca; Jeffrey R Brender; Ayyalusamy Ramamoorthy
Journal:  Biochim Biophys Acta       Date:  2012-08-01

10.  Role of Aromatic Amino Acids in Lipopolysaccharide and Membrane Interactions of Antimicrobial Peptides for Use in Plant Disease Control.

Authors:  Aritreyee Datta; Dipita Bhattacharyya; Shalini Singh; Anirban Ghosh; Artur Schmidtchen; Martin Malmsten; Anirban Bhunia
Journal:  J Biol Chem       Date:  2016-05-02       Impact factor: 5.157
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