Prevention of Amyloid-β Fibril Formation Using Antibodies Against the C-terminal Region of Amyloid-β_1-40 and Amyloid-β_1-42

Article type: Short Communication

Authors: Montañés, María^a | Casabona, Diego^a | Sarasa, Leticia^{b; *} | Pesini, Pedro^{a; b} | Sarasa, Manuel^{a; b}

Affiliations: [a] Araclon Biotech, CIBIR Laboratory, Logroño, Spain | [b] Araclon Biotech, Montecanal Laboratory, Zaragoza, Spain

Correspondence: [*] Correspondence to: Manuel Sarasa, Araclon Biotech, Hospital Montecanal, Franz Schubert 2, 3°, 50012 Zaragoza, Spain. Tel.: +34 876 241 666; Fax: +34 976 020 011; E-mail: msarasa@araclon.com.

Abstract: Alzheimer's disease is characterized by the abnormal aggregation of amyloid-β (Aβ)1-40 and Aβ1-42 peptides into fibrils. In this work, we analyzed the kinetics of Aβ1-40 and Aβ1-42 fibril formation in vitro using Thioflavin T fluorescence. We synthesized high-purity peptides and performed a hexafluoro-2-propanol pre-treatment to yield uniform peptide solutions as starting materials. We found that the aggregation is clearly affected by the presence of sub-millimolar quantities of antibodies against the C-terminal region of the peptides. Because the fibrillization of these peptides is closely related to the pathogenesis of Alzheimer's disease, blocking this process may provide significant therapeutic benefit.

Keywords: Aggregation, Alzheimer's disease, Thioflavin T

DOI: 10.3233/JAD-120850

Journal: Journal of Alzheimer's Disease, vol. 34, no. 1, pp. 133-137, 2013