Stoichiometry and affinity of the human serum albumin-Alzheimer's Aβ peptide interactions.

ABSTRACT: A promising strategy to control the aggregation of the Alzheimer's Aβ peptide in the brain is the clearance of Aβ from the central nervous system into the peripheral blood plasma. Among plasma proteins, human serum albumin plays a critical role in the Aβ clearance to the peripheral sink by binding to Aβ oligomers and preventing further growth into fibrils. However, the stoichiometry and the affinities of the albumin-Aβ oligomer interactions are still to be fully characterized. For this purpose, here we investigate the Aβ oligomer-albumin complexes through a novel and generally applicable experimental strategy combining saturation transfer and off-resonance relaxation NMR experiments with ultrafiltration, domain deletions, and dynamic light scattering. Our results show that the Aβ oligomers

SUBMITTER: Milojevic J 

PROVIDER: S-EPMC3010178 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature