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| - | [[Image:2fbu.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2fbu| PDB=2fbu | SCENE= }} | | {{STRUCTURE_2fbu| PDB=2fbu | SCENE= }} |
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| - | '''Solution structure of the N-terminal fragment of human LL-37'''
| + | ===Solution structure of the N-terminal fragment of human LL-37=== |
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| - | ==Overview==
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| - | To understand the structure and activity relationship of human LL-37, a series of peptide fragments was designed. The N-terminal fragment, LL-37(1-12), was not active, while the C-terminal fragment, LL-37(13-37), killed Escherichia coli, as well as drug-sensitive and drug-resistant cancer cells. A 13-residue core antibacterial and anticancer peptide, corresponding to residues 17-29 of LL-37, was identified based on total correlated spectroscopy by trimming nonessential regions (TOCSY-trim). Because LL-37 acts on bacterial membranes, three-dimensional structures of its fragments were determined in micelles by NMR, including structural refinement by natural abundance 15N and 13C chemical shifts. Aromatic-aromatic interactions in the N-terminal fragment were proposed to be essential for LL-37 aggregation. The LL-37 core peptide adopts a similar structure in the micelles of SDS or dioctanoyl phosphatidylglycerol. This structure is retained in the C-terminal fragment LL-37(13-37) and very likely in intact LL-37 based on peptide-aided signal assignments. The higher antibacterial activity of the LL-37 core peptide than aurein 1.2 was attributed to additional cationic residues. To achieve selective membrane targeting, D-amino acids were incorporated into LL-37(17-32). While the D-peptide showed similar antibacterial activity to the L-diastereomer, it lost toxicity to human cells. Structural analysis revealed hydrophobic defects in the new amphipathic structure of the D-peptide, leading to a much shorter retention time on a reversed-phase HPLC column. It is proposed that hydrophobic defects as a result of incoherent hydrophobic packing provide a structural basis for the improvement in cell selectivity of the LL-37 fragment.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16637646}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16637646 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16637646}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2FBU is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FBU OCA]. | + | 2FBU is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FBU OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Host defense peptide]] | | [[Category: Host defense peptide]] |
| | [[Category: Ll-37]] | | [[Category: Ll-37]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:42:25 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:34:21 2008'' |
Revision as of 05:34, 29 July 2008
Template:STRUCTURE 2fbu
Solution structure of the N-terminal fragment of human LL-37
Template:ABSTRACT PUBMED 16637646
About this Structure
2FBU is a Single protein structure. Full experimental information is available from OCA.
Reference
Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region., Li X, Li Y, Han H, Miller DW, Wang G, J Am Chem Soc. 2006 May 3;128(17):5776-85. PMID:16637646
Page seeded by OCA on Tue Jul 29 08:34:21 2008
