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| - | [[Image:1y58.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1y58| PDB=1y58 | SCENE= }} | | {{STRUCTURE_1y58| PDB=1y58 | SCENE= }} |
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| - | '''The structure of a lactoferricinB derivative bound to micelles'''
| + | ===The structure of a lactoferricinB derivative bound to micelles=== |
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| - | ==Overview==
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| - | The powerful antimicrobial properties of bovine lactoferricin (LfcinB) make it attractive for the development of new antimicrobial agents. An 11-residue linear peptide portion of LfcinB has been reported to have similar antimicrobial activity to lactoferricin itself, but with lower hemolytic activity. The membrane-binding and membrane-perturbing properties of this peptide were studied together with an amidated synthetic version with an added disulfide bond, which was designed to confer increased stability and possibly activity. The antimicrobial and cytotoxic properties of the peptides were measured against Staphylococcus aureus and Escherichia coli and by hemolysis assays. The peptides were also tested in an anti-cancer assay against neuroblastoma cell lines. Vesicle disruption caused by these LfcinB derivatives was studied using the fluorescent reporter molecule calcein. The extent of burial of the two Trp residues in membrane mimetic environments were quantitated by fluorescence. Finally, the solution NMR structures of the peptides bound to SDS micelles were determined to provide insight into their membrane bound state. The cyclic peptide was found to have greater antimicrobial potency than its linear counterpart. Consistent with this property, the two Trp residues of the modified peptide were suggested to be embedded deeper into the membrane. Although both peptides adopt an amphipathic structure without any regular alpha-helical or beta-sheet conformation, the 3D-structures revealed a clearer partitioning of the cationic and hydrophobic faces for the cyclic peptide. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15635665}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15635665 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15635665}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y58 OCA]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y58 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Micelle-bound]] | | [[Category: Micelle-bound]] |
| | [[Category: Peptide]] | | [[Category: Peptide]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:53:32 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:51:56 2008'' |
Revision as of 09:51, 29 July 2008
Template:STRUCTURE 1y58
The structure of a lactoferricinB derivative bound to micelles
Template:ABSTRACT PUBMED 15635665
About this Structure
Full experimental information is available from OCA.
Reference
Structural studies and model membrane interactions of two peptides derived from bovine lactoferricin., Nguyen LT, Schibli DJ, Vogel HJ, J Pept Sci. 2005 Jul;11(7):379-89. PMID:15635665
Page seeded by OCA on Tue Jul 29 12:51:56 2008
