Histidine-containing host-defence skin peptides of anurans bind Cu2+. An electrospray ionisation mass spectrometry and computational modelling study

Tianfang Wang; H J Andreazza; T L Pukala; P J Sherman; A N Calabrese; J H Bowie

doi:10.1002/rcm.4981

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Histidine-containing host-defence skin peptides of anurans bind Cu2+. An electrospray ionisation mass spectrometry and computational modelling study

Journal article

Peer reviewed

Histidine-containing host-defence skin peptides of anurans bind Cu2+. An electrospray ionisation mass spectrometry and computational modelling study

Tianfang Wang, H J Andreazza, T L Pukala, P J Sherman, A N Calabrese and J H Bowie

Rapid Communications in Mass Spectrometry, Vol.25(9), pp.1209-1221

2011

DOI: https://doi.org/10.1002/rcm.4981

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Abstract

Anuran peptides which contain His, including caerin 1.8 (GLFKVLGSVAKHLLPHVVPVIAEKL-NH2), caerin 1.2 (GLLGVLGSVAKHVLPHVVPVIAEHL-NH2), Ala15 maculatin 1.1 (GLFGVLAKVAAHVVAIEHF-NH2), fallaxidin 4.1 (GLLSFLPKVIGHLIHPPS-OH), riparin 5.1 (IVSYPDDAGEHAHKMG-NH2) and signiferin 2.1 (IIGHLIKTALGMLGL-NH2), all form MMet2+ and (M + Met2+-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 metal2+ 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 MCu2+ complexes with the membrane active caerin 1.8, Ala15 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).

Details

Title: Histidine-containing host-defence skin peptides of anurans bind Cu2+. An electrospray ionisation mass spectrometry and computational modelling study
Authors: Tianfang Wang (Author) - University of Adelaide
H J Andreazza (Author) - University of Adelaide
T L Pukala (Author) - University of Adelaide
P J Sherman (Author) - University of Adelaide
A N Calabrese (Author) - University of Adelaide
J H Bowie (Author) - University of Adelaide
Publication details: Rapid Communications in Mass Spectrometry, Vol.25(9), pp.1209-1221
Publisher: John Wiley & Sons Ltd.
Date published: 2011
DOI: 10.1002/rcm.4981
ISSN: 0951-4198
Organisation Unit: School of Science and Engineering - Legacy; University of the Sunshine Coast, Queensland; School of Science, Technology and Engineering; Centre for Bioinnovation
Language: English
Record Identifier: 99450141102621
Output Type: Journal article

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