2ox2
From Proteopedia
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'''Structure of the cantionic, antimicrobial hexapeptide cyclo(RRWWFR) bound to DPC-micelles''' | '''Structure of the cantionic, antimicrobial hexapeptide cyclo(RRWWFR) bound to DPC-micelles''' | ||
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[[Category: Soderhall, J A.]] | [[Category: Soderhall, J A.]] | ||
[[Category: Wessolowski, A.]] | [[Category: Wessolowski, A.]] | ||
| - | [[Category: | + | [[Category: Antimicrobial]] |
| - | [[Category: | + | [[Category: Antimicrobial protein]] |
| - | [[Category: | + | [[Category: Cationic peptide]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:50:47 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:50, 4 May 2008
Structure of the cantionic, antimicrobial hexapeptide cyclo(RRWWFR) bound to DPC-micelles
Overview
New antimicrobial compounds are of major importance because of the growing problem of bacterial resistance. In this context, antimicrobial peptides have received a lot of attention. Their mechanism of action, however, is often obscure. Here, the structures of two cyclic, antimicrobial peptides from the family of arginine- and tryptophan-rich peptides determined in a membrane-mimicking environment are described. The sequence of the peptides has been obtained from a cyclic parent peptide by scrambling the amino acids. While the activity of the peptides is similar to that of the parent peptide, the structures are not. The peptides do, however, all adopt an amphiphilic structure. A comparison between the structures helps to define the requirements for the activity of these peptides. Copyright (c) 2007 European Peptide Society and John Wiley & Sons, Ltd.
About this Structure
Full crystallographic information is available from OCA.
Reference
Structures of cyclic, antimicrobial peptides in a membrane-mimicking environment define requirements for activity., Appelt C, Wessolowski A, Dathe M, Schmieder P, J Pept Sci. 2007 Nov 6;. PMID:17985394 Page seeded by OCA on Sun May 4 11:50:47 2008
