TAILIEUCHUNG - Báo cáo khoa học: Discrete conformational changes as regulators of the hydrolytic properties of beta-amyloid (1–40)

Beta-amyloid (1–40) (Abeta), the main component of senile plaques seen in the brains of Alzheimer’s disease patients, was found to be toxic both as fibrils and smaller soluble globular aggregates. The hydrolytic properties of Abeta, a new biochemical activity described previously [Brzyska M, Bacia A & Elbaum D (2001)Eur J Biochem268, 3443–3454], may contribute to its overall toxicity. | ễFEBS Journal Discrete conformational changes as regulators of the hydrolytic properties of beta-amyloid 1-40 Maria Brzyska1 Katarzyna Trzesniewska1 Tomasz Gers2 and Danek Elbaum1 1 Laboratory of Bio-PhysicalMethods Nencki Institute of ExperimentalBiology Polish Academy of Sciences Warsaw Poland 2 Chemistry Department Warsaw University Poland Keywords beta-amyloid 1-40 ester hydrolysis conformation hydrophobicity oligomerization Correspondence M. Brzyska Laboratory of Bio-Physical Methods Nencki Institute of Experimental Biology Polish Academy of Sciences Pasteura 3 02-093 Warsaw Poland Fax 48 22 822 52 43 Tel 48 22 589 24 79 E-mail Received 15 September 2006 accepted 20 October 2006 doi Beta-amyloid 1-40 Abeta the main component of senile plaques seen in the brains of Alzheimer s disease patients was found to be toxic both as fibrils and smaller soluble globular aggregates. The hydrolytic properties of Abeta a new biochemical activity described previously Brzyska M Bacia A Elbaum D 2001 Eur J Biochem 268 3443-3454 may contribute to its overall toxicity. In this study the hydrolysis of fluorescein ester series was studied under predetermined conditions affecting Abeta hydrophobicity and conformation. Reaction products of the most effectively decomposed ester dibutyrate were characterized using HPLC and ESI-MS. Hydrophobicity of Abeta as measured by bis-8-anilinonaphthalene fluorescence correlated with its hydrolytic abilities. FTIR and CD data analysis showed a relationship between enhanced hydrolytic abilities and Abeta structure. Seriously limited hydrolysis caused by higher peptide concentrations is consistent with monomeric dimeric Abeta species participation in the process confirmed by thioflavine T binding. Inhibition of hydrolysis was caused by b-sheet breaker peptide LPFFD indicating that the Abeta central hydrophobic cluster amino acids 17-21 participates in the process. The reported Abeta properties

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