SABINA BANCILA, OLGA PINTILIE, ROBERT GRADINARU, ION SANDU, GABI DROCHIOIU, GHEORGHE G. BALANInteraction of Heavy Metal Ions with Glycyl-L-tryptophan in the Presence of Amyloid-b Peptides<br>Interaction of Heavy Metal Ions with Glycyl-L-tryptophan in the Presence of Amyloid-b Peptides

SABINA BANCILA, OLGA PINTILIE, ROBERT GRADINARU, ION SANDU, GABI DROCHIOIU, GHEORGHE G. BALANInteraction of Heavy Metal Ions with Glycyl-L-tryptophan in the Presence of Amyloid-b Peptides
Interaction of Heavy Metal Ions with Glycyl-L-tryptophan in the Presence of Amyloid-b Peptides

Abstract:

Metal complexes of amyloid-b peptides (Ab), associated with Alzheimer’s disease (AD), are increasingly investigated, being involved in toxic oligomer formation and fibrillogenesis. The metal ions such as copper, zinc, and iron have been shown to be involved in AD, being found in the amyloid plaques of AD brains. Here we studied the interaction of Cu2+, Ni2+, Ag+, and Hg2+ ions with amyloid-b-peptide 1-40 (Ab1-40), measuring the fluorescence of glycyl-L-tryptophan (GW) peptide added to metal-peptide complex solutions. Only some heavy metal ions proved to be quenchers of the fluorescent peptide GW, whereas Ab peptide interfered with their fluorescence quenching alongside with the formation of metal-Ab complexes. While copper ions decreased the fluorescence intensity of the GW peptide, nickel ions did not quench it. Silver did not influence much the GW fluorescence, while mercury had contrary effects depending on its concentration and the GW concentration. Moreover, its effect on the GW fluorescence was more influenced by the presence of Ab peptide. Keywords: glycyl-L-tryptophan; heavy metal ions; amyloid-b peptide; fibrillogenesis; fluorescence

Issue: 2016, Volume 67, Issue 5

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