Alzheimer's β‐amyloid peptide: affinity for metal chelates

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Abstract
Alzheimer's amyloid peptide, Aβ(1-42) and its fragments, Aβ(1-28) and Aβ(1-16), were chromatographed on IDA-M(II) columns (M: Cu2+, Ni2+ and Zn2+). The retention of Aβ(1-42) and its fragments on IDA-Cu(II) could not be reversed in decreasing a gradient of pH, from 7.0 to 4.0. All Aβ peptides were recovered from IDA-Ni(II) columns in a decreasing pH gradient from 7.0 to 4.0, within the pH range from 5.6 to 5.1. Aβ(1-42) peptide was strongly retained on IDA-Zn(II) at pH 4.0, but it's aβ(1-28) and Aβ(1-16) were only transiently retained on IDA-Zn(II) columns when applied at pH 6.1. We submit that histidine clusters, residing both in the Alzheimer's β-amyloid peptide and in most of the APP/APLP superfamily of proteins, constitute high-affinity binding sites for immobilized metal chelates.

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