Abstract : The data here consists of calcium imaging of human neuro-blastoma SH-SY5Y cells treated with the calcium-sensitive dye Fluo-4AM and then incubated with nanomolar concentrations of either human or rat Alzheimer's β-amyloid peptide Aβ1-42. These data are both of a qualitative (fluorescence micrographs) and semi-quantitative nature (estimation of intracellular calcium concentrations of cells probed by Aβ1-42 peptides vs. control untreated cells). Since rat Aβ1-42 differs from its human counterpart at only three amino acid positions, this comparative study is a good assessment of the specificity of the amyloid pore forming assay. The interpretation of this dataset is presented in the accompanying study " Broad neutralization of calcium-permeable amyloid pore channels with a chimeric Alzheimer/Parkinson pep-tide targeting brain gangliosides " [1].
Coralie Di Scala, Nouara yahi, Alessandra Flores, Sonia Boutemeur, Nazim Kourdougli, et al.. Comparison of the amyloid pore forming properties of rat and human Alzheimer’s beta-amyloid peptide 1-42: Calcium imaging data. Data in Brief, Elsevier, 2014, 6, pp.640-643. ⟨10.1016/j.dib.2016.01.019⟩. ⟨hal-01768262⟩