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https://hdl.handle.net/2440/71091
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dc.contributor.author | Wang, T. | - |
dc.contributor.author | Andreazza, H. | - |
dc.contributor.author | Pukala, T. | - |
dc.contributor.author | Sherman, P. | - |
dc.contributor.author | Calabrese, A. | - |
dc.contributor.author | Bowie, J. | - |
dc.date.issued | 2011 | - |
dc.identifier.citation | Rapid Communications in Mass Spectrometry, 2011; 25(9):1209-1221 | - |
dc.identifier.issn | 0951-4198 | - |
dc.identifier.issn | 1097-0231 | - |
dc.identifier.uri | http://hdl.handle.net/2440/71091 | - |
dc.description.abstract | Anuran peptides which contain His, including caerin 1.8 (GLFKVLGSVAKHLLPHVVPVIAEKL-NH(2)), caerin 1.2 (GLLGVLGSVAKHVLPHVVPVIAEHL-NH(2)), Ala(15) maculatin 1.1 (GLFGVLAKVAAHVVAIEHF-NH(2)), fallaxidin 4.1 (GLLSFLPKVIGHLIHPPS-OH), riparin 5.1 (IVSYPDDAGEHAHKMG-NH(2)) and signiferin 2.1 (IIGHLIKTALGMLGL-NH(2)), all form MMet(2+) and (M + Met(2+)-2H(+))(2+) cluster ions (where Met is Cu, Mg and Zn) following electrospray ionisation (ESI) in a Waters QTOF 2 mass spectrometer. Peaks due to Cu(II) complexes are always the most abundant relative to other metal complexes. Information concerning metal(2+) connectivity in a complex has been obtained (at least in part) using b and y fragmentation data from ESI collision-induced dissociation tandem mass spectrometry (CID MS/MS). Theoretical calculations, using AMBER version 10, show that MCu(2+) complexes with the membrane active caerin 1.8, Ala(15) maculatin 1.1 and fallaxidin 4.1 are four-coordinate and approximating square planar, with ligands including His and Lys, together with the carbonyl oxygens of particular backbone amide groups. When binding can occur through two His, or one His and one Lys, the His/Lys ligand structure is the more stable for the studied systems. The three-dimensional (3D) structures of the complexes are always different from the previously determined structures of the uncomplexed model peptides (using 2D nuclear magnetic resonance (NMR) spectroscopy in membrane-mimicking solvents like trifluoroethanol/water). | - |
dc.description.statementofresponsibility | Tianfang Wang, Hayley J. Andreazza, Tara L. Pukala, Patrick J. Sherman, Antonio N. Calabrese and John H. Bowie | - |
dc.language.iso | en | - |
dc.publisher | John Wiley & Sons Ltd | - |
dc.rights | Copyright © 2011 John Wiley & Sons, Ltd. | - |
dc.source.uri | http://dx.doi.org/10.1002/rcm.4981 | - |
dc.subject | Animals | - |
dc.subject | Anura | - |
dc.subject | Metals, Heavy | - |
dc.subject | Copper | - |
dc.subject | Histidine | - |
dc.subject | Antimicrobial Cationic Peptides | - |
dc.subject | Amphibian Proteins | - |
dc.subject | Circular Dichroism | - |
dc.subject | Nuclear Magnetic Resonance, Biomolecular | - |
dc.subject | Spectrometry, Mass, Electrospray Ionization | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Protein Binding | - |
dc.subject | Molecular Sequence Data | - |
dc.subject | Disk Diffusion Antimicrobial Tests | - |
dc.subject | Molecular Dynamics Simulation | - |
dc.title | Histidine-containing host-defence skin peptides of anurans bind Cu²⁺. An electrospray ionisation mass spectrometry and computational modelling study | - |
dc.title.alternative | Histidine-containing host-defence skin peptides of anurans bind Cu(2+). An electrospray ionisation mass spectrometry and computational modelling study | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1002/rcm.4981 | - |
dc.relation.grant | ARC | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Pukala, T. [0000-0001-7391-1436] | - |
Appears in Collections: | Aurora harvest Chemistry publications |
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