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| | ==SOLUTION NMR STRUCTURE OF MAXIMIN 1 IN 50% TRIFLUOROETHANOL== | | ==SOLUTION NMR STRUCTURE OF MAXIMIN 1 IN 50% TRIFLUOROETHANOL== |
| - | <StructureSection load='7ovz' size='340' side='right'caption='[[7ovz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='7ovz' size='340' side='right'caption='[[7ovz]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7ovz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OVZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7ovz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombina_maxima Bombina maxima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OVZ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6hz2|6hz2]]</div></td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ovz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ovz OCA], [https://pdbe.org/7ovz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ovz RCSB], [https://www.ebi.ac.uk/pdbsum/7ovz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ovz ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ovz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ovz OCA], [https://pdbe.org/7ovz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ovz RCSB], [https://www.ebi.ac.uk/pdbsum/7ovz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ovz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/M1H1_BOMMX M1H1_BOMMX]] Maximin-1 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans, but not against A.flavus nor P.uticale. It has little hemolytic activity. It possess a significant cytotoxicity against tumor cell lines. It does not possess a significant anti-HIV activity. It shows high spermicidal activity.<ref>PMID:15770703</ref> Maximin-H1 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity.<ref>PMID:15770703</ref>
| + | [https://www.uniprot.org/uniprot/M1H1_BOMMX M1H1_BOMMX] Maximin-1 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans, but not against A.flavus nor P.uticale. It has little hemolytic activity. It possess a significant cytotoxicity against tumor cell lines. It does not possess a significant anti-HIV activity. It shows high spermicidal activity.<ref>PMID:15770703</ref> Maximin-H1 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity.<ref>PMID:15770703</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Bombina maxima]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hewage, C M]] | + | [[Category: Hewage CM]] |
| - | [[Category: Timmons, P B]] | + | [[Category: Timmons PB]] |
| - | [[Category: Antimicrobial peptide]]
| + | |
| - | [[Category: Antimicrobial protein]]
| + | |
| - | [[Category: Maximin 1]]
| + | |
| Structural highlights
Function
M1H1_BOMMX Maximin-1 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans, but not against A.flavus nor P.uticale. It has little hemolytic activity. It possess a significant cytotoxicity against tumor cell lines. It does not possess a significant anti-HIV activity. It shows high spermicidal activity.[1] Maximin-H1 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity.[2]
Publication Abstract from PubMed
Maximin 1 is a cationic, amphipathic antimicrobial peptide found in the skin secretions and brains of the Chinese red belly toad Bombina maxima. The 27 amino acid residue-long peptide is biologically interesting as it possesses a variety of biological activities, including antibacterial, antifungal, antiviral, antitumour and spermicidal activities. Its three-dimensional structural model was obtained in a 50/50% water/2,2,2-trifluoroethanol-d3 mixture using two-dimensional NMR spectroscopy. Maximin 1 was found to adopt an alpha-helical structure from residue Ile(2) to Ala(26) . The peptide is amphipathic, showing a clear separation between polar and non-polar residues. The interactions with sodium dodecyl sulfate micelles, a widely-used bacterial membrane-mimicking environment, were modelled using molecular dynamics simulations. The peptide maintains an alpha-helical conformation, occasionally displaying a flexibility around the Gly(9) and Gly(16) residues, which is likely responsible for the peptide's low haemolytic activity. It is found to preferentially adopt a position parallel to the micellar surface, establishing a number of hydrophobic and electrostatic interactions with the micelle.
Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1.,Timmons PB, Hewage CM J Pept Sci. 2021 Sep 26:e3370. doi: 10.1002/psc.3370. PMID:34569121[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. Eur J Immunol. 2005 Apr;35(4):1220-9. doi: 10.1002/eji.200425615. PMID:15770703 doi:http://dx.doi.org/10.1002/eji.200425615
- ↑ Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. Eur J Immunol. 2005 Apr;35(4):1220-9. doi: 10.1002/eji.200425615. PMID:15770703 doi:http://dx.doi.org/10.1002/eji.200425615
- ↑ Timmons PB, Hewage CM. Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1. J Pept Sci. 2021 Sep 26:e3370. doi: 10.1002/psc.3370. PMID:34569121 doi:http://dx.doi.org/10.1002/psc.3370
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