It is widely accepted that Pb(II), a non-essential metal ion, can lead to one of the most preventable public health concerns in the US. Although the use of lead in materials such as paint and gasoline was phased out starting in the 1970s, the elimination of childhood lead poisoning is still one of the goals of the CDC’s Healthy People 2020 initiative. Various metalloproteins, such as the membrane trafficking protein synaptotagmin-1 (syt1), have been shown to bind lead with a greater affinity than Ca(II) and identified as a potential target for lead. One proposal is that upon Ca(II) binding syt1 undergoes structural changes necessary to facilitate its role in membrane fusion. In the presence of Pb(II) it is possible that structural changes are not fully induced and proper membrane fusion will not take place. Using spectroscopic and calorimetric approaches we have endeavored to determine structural differences between Ca(II) and Pb(II) bound syt1. A better understanding of the structural differences may elucidate the reason(s) behind loss in function of syt1 when Pb(II) binds.

Probing the structural difference between Ca(II) and Pb(II) bound syt1

251st National Meeting (2016)

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