European Journal of Mass Spectrometry 2007-01-01

Copper-induced oligomerization of peptides: a model study.

Gitta Schlosser, Raluca Stefanescu, Michael Przybylski, Manuela Murariu, Ferenc Hudecz, Gabi Drochioiu

Index: Eur. J. Mass Spectrom. (Chichester, Eng.) 13(5) , 331-7, (2007)

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Abstract

In this work, copper-binding of the tetraglycine peptide (Gly-Gly-Gly-Gly) was studied by electrospray ionization mass spectrometry. Experiments were performed under alkaline conditions, in the presence of ethanolamine (pH 10.95). We observed that the presence of copper(II) ions induces the aggregation of the peptide and the formation of copper-bound complexes with higher molecular mass is favored, such as the oligomer complexes [3M+2Cu-3H](+) and [4M+3Cu-5H](+). At 1:1 peptide-copper(II) ion ratio, the singly charged [3M+2Cu-3H](+) oligomer complex is the base peak in the mass spectrum. Metal ion-induced oligomer-ization of neurotoxic peptides is well known in the literature; however, there are very few examples in which such oligomerization was directly observed by mass spectrometry. Our results show that application of short peptides can be useful to study the -mechanism of metal ion binding and metal ion-induced oligomerization of peptides.

Related Compounds

Structure Name/CAS No. Articles
H-Gly-Gly-Gly-Gly-OH Structure H-Gly-Gly-Gly-Gly-OH
CAS:637-84-3