2ox2
From Proteopedia
(New page: 200px<br /><applet load="2ox2" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ox2" /> '''Structure of the cantionic, antimicrobial he...) |
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==Overview== | ==Overview== | ||
| - | New antimicrobial compounds are of major importance because of the growing | + | 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== | ==About this Structure== | ||
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[[Category: Dathe, M.]] | [[Category: Dathe, M.]] | ||
[[Category: Schmieder, P.]] | [[Category: Schmieder, P.]] | ||
| - | [[Category: Soderhall, J | + | [[Category: Soderhall, J A.]] |
[[Category: Wessolowski, A.]] | [[Category: Wessolowski, A.]] | ||
[[Category: antimicrobial]] | [[Category: antimicrobial]] | ||
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[[Category: cationic peptide]] | [[Category: cationic peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:23:28 2008'' |
Revision as of 16:23, 21 February 2008
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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
2OX2 is a Protein complex structure of sequences from [1]. 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
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