Studying transition metal-binding sites in β-2-microglobulin and their influences on its aggregation using MCO-MS and SEC-MS

摘要

1. Cu(II) binding to β2m causes the protein to initially form oligomers (i.e., dimers, tetramers and hexamers) and eventually to form fibrils; 2. Ni(II) binds to β2m primarily at N-terminus and His31 as revealed by MCO-MS data, however, oligomerization is absent in the presence of Ni(II). Detailed structural changes induced by Ni(II) will be further elucidated by H/D exchange; 3. The binding sites and the progression of β2m oligomerization in the presence of Zn(II) will be further investigated to provide a clearer picture of the metal-protein interactions that are necessary to lead to β2m amyloid formation.