1xv4: Difference between revisions

Revision as of 16:58, 21 February 2008

Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in SDS micelles

OverviewOverview

Treatment of Gram-negative bacterial infections with antimicrobial agents can cause release of the endotoxin lipopolysaccharide (LPS), the potent initiator of sepsis, which is the major cause of mortality in intensive care units worldwide. Structural information on peptides bound to LPS can lead to the development of more effective endotoxin neutralizers. Short linear antimicrobial and endotoxin-neutralizing peptide LF11, based on the human lactoferrin, binds to LPS, inducing a peptide fold with a "T-shaped" arrangement of a hydrophobic core and two clusters of basic residues that match the distance between the two phosphate groups of LPS. Side chain arrangement of LF11 bound to LPS extends the previously proposed LPS binding pattern, emphasizing the importance of both electrostatic and hydrophobic interactions in a defined geometric arrangement. In anionic micelles, the LF11 forms amphipathic conformation with a smaller hydrophobic core than in LPS, whereas in zwitterionic micelles, the structure is even less defined. Protection of tryptophan fluorescence quenching in the order SDS>LPS>DPC and hydrogen exchange protection indicates the decreasing extent of insertion of the N terminus and potential role of peptide plasticity in differentiation between bacterial and eukaryotic membranes.

About this StructureAbout this Structure

1XV4 is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide., Japelj B, Pristovsek P, Majerle A, Jerala R, J Biol Chem. 2005 Apr 29;280(17):16955-61. Epub 2005 Feb 1. PMID:15687491

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-[[Image:1xv4.gif|left|200px]]<br /><applet load="1xv4" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1xv4" />
 '''Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in SDS micelles'''<br />
 ==Overview==
-Treatment of Gram-negative bacterial infections with antimicrobial agents, can cause release of the endotoxin lipopolysaccharide (LPS), the potent, initiator of sepsis, which is the major cause of mortality in intensive, care units worldwide. Structural information on peptides bound to LPS can, lead to the development of more effective endotoxin neutralizers. Short, linear antimicrobial and endotoxin-neutralizing peptide LF11, based on the, human lactoferrin, binds to LPS, inducing a peptide fold with a "T-shaped", arrangement of a hydrophobic core and two clusters of basic residues that, match the distance between the two phosphate groups of LPS. Side chain, arrangement of LF11 bound to LPS extends the previously proposed LPS, binding pattern, emphasizing the importance of both electrostatic and, hydrophobic interactions in a defined geometric arrangement. In anionic, micelles, the LF11 forms amphipathic conformation with a smaller, hydrophobic core than in LPS, whereas in zwitterionic micelles, the, structure is even less defined. Protection of tryptophan fluorescence, quenching in the order SDS&gt;LPS&gt;DPC and hydrogen exchange protection, indicates the decreasing extent of insertion of the N terminus and, potential role of peptide plasticity in differentiation between bacterial, and eukaryotic membranes.
+Treatment of Gram-negative bacterial infections with antimicrobial agents can cause release of the endotoxin lipopolysaccharide (LPS), the potent initiator of sepsis, which is the major cause of mortality in intensive care units worldwide. Structural information on peptides bound to LPS can lead to the development of more effective endotoxin neutralizers. Short linear antimicrobial and endotoxin-neutralizing peptide LF11, based on the human lactoferrin, binds to LPS, inducing a peptide fold with a "T-shaped" arrangement of a hydrophobic core and two clusters of basic residues that match the distance between the two phosphate groups of LPS. Side chain arrangement of LF11 bound to LPS extends the previously proposed LPS binding pattern, emphasizing the importance of both electrostatic and hydrophobic interactions in a defined geometric arrangement. In anionic micelles, the LF11 forms amphipathic conformation with a smaller hydrophobic core than in LPS, whereas in zwitterionic micelles, the structure is even less defined. Protection of tryptophan fluorescence quenching in the order SDS&gt;LPS&gt;DPC and hydrogen exchange protection indicates the decreasing extent of insertion of the N terminus and potential role of peptide plasticity in differentiation between bacterial and eukaryotic membranes.
 ==About this Structure==
-XV4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XV4 OCA].
+XV4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XV4 OCA].
 ==Reference==
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