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| [[Image:1d9j.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1d9j.png|left|200px]] |
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| {{STRUCTURE_1d9j| PDB=1d9j | SCENE= }} | | {{STRUCTURE_1d9j| PDB=1d9j | SCENE= }} |
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| '''SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE'''
| | ===SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE=== |
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| ==Overview==
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| In order to elucidate the structure-antibiotic activity relationships of the peptides, the three-dimensional structures of two hybrid peptides, CA(1-8) - MA(1-12) and CA(1-8) - ME(1-12) in trifluoroethanol-containing aqueous solution were investigated by NMR spectroscopy. Both CA(1-8) - MA(1-12) and CA(1-8) - ME(1-12) have strong antibacterial activity but only CA(1-8) - ME(1-12) has hemolytic activity against human erythrocytes. CA(1-8) - MA(1-12) has a hydrophobic 310-helix of only two turns combined with one short helix in the N-terminus with a flexible hinge section in between. CA(1-8) - MA(1-12) has a severely bent structure in the middle of the peptide. These structural features as well as the low hydrophobicity of CA(1-8) - MA(1-12) seem to be crucial for the selective lysis against the membrane of prokaryotic cells. CA(1-8) - ME(1-12) has an alpha-helical structure of about three turns in the melittin domain and a flexible structure with one turn in the cecropin domain connected with a flexible hinge section in between, and these might be the structural features required for membrane disruption against prokaryotic and eukaryotic cells. The central hinge region (Gly9-Ile10-Gly11) in an amphipathic antibacterial peptide is considered to play an important role in providing the conformational flexibility required for ion channel formation of the C-terminal hydrophobic alpha-helix on cell membrane.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10424354}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10424354 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10424354}} |
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| ==About this Structure== | | ==About this Structure== |
| 1D9J is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9J OCA]. | | 1D9J is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9J OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Oh, D.]] | | [[Category: Oh, D.]] |
| [[Category: Helix-hinge-helix]] | | [[Category: Helix-hinge-helix]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:36:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:42:37 2008'' |
