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The capacity of albumin to bind to beta-amyloid

M. Costa, A.M. Ortiz, J.I. Jorquera [REV NEUROL 2010;50 (Supl. 5):S1-S4] PMID: 20517864 DOI: https://doi.org/10.33588/rn.50S05.2010083

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Volumen 50 | Number S05 | Nº of views of the article 6.734 | Nº of PDF downloads 723 | Article publication date 16/03/2010

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ABSTRACT

INTRODUCTION Most plasma beta-amyloid peptide (Aß) has been described to circulate bound to albumin (aprox. 90%). Moreover, a balance between peripheral and brain Aß seems to exist, so a reduction of Aß levels in blood through plasma exchange with therapeutic albumin should induce a clearance of brain Aß. In this study, content of Aß in therapeutic albumin as well as its binding capacity were characterized.

MATERIALS AND METHODS Levels of Aß(1-40) and Aß(1-42) were determined by means of ELISA technique in therapeutic albumin (human albumin Grifols; n = 18 batches), in normal plasma (n = 8) and in plasma from patients with Alzheimer disease (n = 45). Binding capacity of therapeutic albumin to synthetic peptides containing the primary sequence of human Aß(1-42) was determined by means of surface plasmon resonance (SPR) technique.

RESULTS Both the Aß(1-40) and Aß(1-42) levels in therapeutic albumin were always lower than the last valid point measured in the standard curve (< 25 to < 63 pg/mL). Levels in normal plasma and in plasma from Alzheimer disease patients ranged between < 25 to 312 pg/mL for Aß(1-40), and < 25 to 279,4 pg/mL for Aß(1-42). SPR studies confirmed the high affinity of therapeutic albumin for the experimental Aß peptide.

CONCLUSIONS Human albumin Grifols shows undetectable Aß levels, and lower to those observed in normal plasma and in plasma from patients with Alzheimer diisease. Moreover, it was able to bind peptides containing the sequence of human Aß(1-42). KeywordsAlbumin Alzheimer disease Beta-amyloid peptide CategoriesDemencia Neurodegeneración

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The capacity of albumin to bind to beta-amyloid