Cross interaction of β-amyloid peptide and prion protein fragments

Abstract

This article presents kinetic studies of cross interaction ofβ-amyloid peptide and prion protein fragments. Synthesesof three peptides (β25–35, β22–35 and PrP 109–126) were performed. Those peptides were used for aggregation studies in PBS and TRIS buffers using HPLC with DAD detector. Comparison of aggregation of peptides alone and incombination with other fragments was investigated. In all cases aggregation was faster in PBS than in TRIS solution. Obtained results suggest that β-amyloid peptide and prion protein may interact to form macromolecular complexes with different ability for aggregation.