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2k10
From Proteopedia
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'''Confirmational analysis of the broad-spectrum antibacterial peptide, rantuerin-2csa: identification of a full length helix-turn-helix motif''' | '''Confirmational analysis of the broad-spectrum antibacterial peptide, rantuerin-2csa: identification of a full length helix-turn-helix motif''' | ||
| + | |||
| + | ==Overview== | ||
| + | Design of clinically valuable antibacterial agents based upon naturally occurring peptides requires the use of spectroscopic methods, particularly NMR, to determine the three-dimensional structure of the native peptide so that analogues with improved therapeutic properties can be made. Ranatuerin-2CSa (GILSSFKGVAKGVAKDLAG KLLETLKCKITGC), first isolated from skin secretions of the Cascades frog, Rana cascadae, represents a promising candidate for drug development. The peptide shows potent growth inhibitory activity against Escherichia coli (MIC=5 muM) and Staphylococcus aureus (MIC=10 muM) but displays haemolytic activity against human erythrocytes (LC(50)=160 muM). The solution structure of ranatuerin-2CSa was investigated by proton NMR spectroscopy and molecular modelling. In aqueous solution, the peptide lacks secondary structure but, in a 2,2,2-trifluoroethanol (TFE-d(3))-H(2)O solvent mixture, the structure is characterised by a full length helix-turn-helix conformation between residues I(2)-L(21), L(22)-L(25) and K(26)-T(30) respectively. This structural information will facilitate the design of novel therapeutic agents based upon the ranatuerin-2CSa structure with improved antimicrobial potencies but decreased cytolytic activities against mammalian cells. | ||
==About this Structure== | ==About this Structure== | ||
2K10 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K10 OCA]. | 2K10 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K10 OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | Conformational analysis of the broad-spectrum antibacterial peptide, ranatuerin-2CSa: Identification of a full length helix-turn-helix motif., Subasinghage AP, Conlon JM, Hewage CM, Biochim Biophys Acta. 2008 Jun;1784(6):924-9. Epub 2008 Mar 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18387372 18387372] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Conlon, M.]] | [[Category: Conlon, M.]] | ||
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[[Category: Molecular modelling]] | [[Category: Molecular modelling]] | ||
[[Category: Nmr]] | [[Category: Nmr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 4 09:57:56 2008'' |
Revision as of 06:57, 4 June 2008
Confirmational analysis of the broad-spectrum antibacterial peptide, rantuerin-2csa: identification of a full length helix-turn-helix motif
Overview
Design of clinically valuable antibacterial agents based upon naturally occurring peptides requires the use of spectroscopic methods, particularly NMR, to determine the three-dimensional structure of the native peptide so that analogues with improved therapeutic properties can be made. Ranatuerin-2CSa (GILSSFKGVAKGVAKDLAG KLLETLKCKITGC), first isolated from skin secretions of the Cascades frog, Rana cascadae, represents a promising candidate for drug development. The peptide shows potent growth inhibitory activity against Escherichia coli (MIC=5 muM) and Staphylococcus aureus (MIC=10 muM) but displays haemolytic activity against human erythrocytes (LC(50)=160 muM). The solution structure of ranatuerin-2CSa was investigated by proton NMR spectroscopy and molecular modelling. In aqueous solution, the peptide lacks secondary structure but, in a 2,2,2-trifluoroethanol (TFE-d(3))-H(2)O solvent mixture, the structure is characterised by a full length helix-turn-helix conformation between residues I(2)-L(21), L(22)-L(25) and K(26)-T(30) respectively. This structural information will facilitate the design of novel therapeutic agents based upon the ranatuerin-2CSa structure with improved antimicrobial potencies but decreased cytolytic activities against mammalian cells.
About this Structure
2K10 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Conformational analysis of the broad-spectrum antibacterial peptide, ranatuerin-2CSa: Identification of a full length helix-turn-helix motif., Subasinghage AP, Conlon JM, Hewage CM, Biochim Biophys Acta. 2008 Jun;1784(6):924-9. Epub 2008 Mar 14. PMID:18387372 Page seeded by OCA on Wed Jun 4 09:57:56 2008
