- Longitudinal Neuroimaging Analysis in Mild-Moderate Alzheimer's Disease Patients Treated with Plasma Exchange with 5% Human Albumin. [Journal Article]
- JAJ Alzheimers Dis 2018; 61(1):321-332
- CONCLUSIONS: Mild-moderate AD patients showed decreased brain volume and impairment of brain perfusion as expected for the progression of the disease. PE-treatment with albumin replacement favored the stabilization of perfusion.
- Efficacy and Safety of Plasma Exchange with 5% Albumin to Modify Cerebrospinal Fluid and Plasma Amyloid-β Concentrations and Cognition Outcomes in Alzheimer's Disease Patients: A Multicenter, Randomized, Controlled Clinical Trial. [Journal Article]
- JAJ Alzheimers Dis 2017; 56(1):129-143
- CONCLUSIONS: PE with human albumin modified CSF and plasma Aβ1-42 levels. Patients treated with PE showed improvement in memory and language functions, which persisted after PE was discontinued.
- Treatment of Alzheimer disease using combination therapy with plasma exchange and haemapheresis with albumin and intravenous immunoglobulin: Rationale and treatment approach of the AMBAR (Alzheimer Management By Albumin Replacement) study. [Review]
- NNeurologia 2016; 31(7):473-81
- CONCLUSIONS: the AMBAR study represents a new therapeutic perspective for AD.
- In vitro amyloid-β binding and inhibition of amyloid-β self-association by therapeutic albumin. [Journal Article]
- JAJ Alzheimers Dis 2014; 38(4):753-65
- CONCLUSIONS: Albutein inhibited Aβ self-association by selectively binding Aβ aggregates rather than monomers and by preventing further growth of the Aβ assemblies.
- Therapeutic albumin binding to remove amyloid-β. [Journal Article]
- JAJ Alzheimers Dis 2012; 29(1):159-70
- Clearance of plasma amyloid-β (Aβ) through plasma exchange and replacement with therapeutic albumin to facilitate net Aβ efflux from the brain to plasma is a novel approach for the treatment of Alzhe...
Clearance of plasma amyloid-β (Aβ) through plasma exchange and replacement with therapeutic albumin to facilitate net Aβ efflux from the brain to plasma is a novel approach for the treatment of Alzheimer's disease. Therefore, thorough characterization of the capacity of therapeutic albumin to bind Aβ is warranted. In this study, Aβ40 and Aβ42 were quantified by commercial ELISA or Araclon ABtest® in samples of Grifols' therapeutic albumin (Albutein®) 5%, 20%, and 25%. The capacity of Albutein® to bind Aβ was assessed by: a) ELISA in serially diluted therapeutic albumin (0-45 mg/ml protein concentration) to which 80 pg/ml of synthetic Aβ peptide (sAβ40 or sAβ42) were added; b) ELISA in samples of the therapeutic albumin containing serially diluted sAβ40 or sAβ42 (60-400 pg/ml); and c) surface plasmon resonance (SPR) for sAβ42 binding. The Aβ content in Albutein® was below the quantification threshold of the ELISA tests (<25 to <62.5 pg/ml) and ABtest® (<3.125 pg/ml). Quantification of exogenously added sAβ42 decreased in parallel with increasing protein concentration (59-78% at 45 mg/ml albumin). Recovery of sAβ serially diluted in Albutein® was ∼60% for sAβ40 and ∼70% for sAβ42, but was ∼100% in control samples without albumin. The KD by SPR analysis for sAβ42 interaction with Albutein® was 1.72 ± 0.24 × 10-6 M. In conclusion, Grifols' therapeutic albumin has undetectable content of Aβ40 and Aβ42. Moreover, Grifols' therapeutic albumin consistently binds peptides containing the primary sequence of human Aβ.