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Binding of an Oxindole Alkaloid from Uncaria tomentosa to Amyloid Protein (Aβ1-40)

Author:
Frąckowiak, Teresa, Bączek, Tomasz, Kaliszan, Roman, Żbikowska, Beata, Gleńsk, Michał, Fecka, Izabela, Cisowski, Wojciech
Source:
Zeitschrift für Naturforschung 2014 v.61 no.11-12 pp. 821-826
ISSN:
1865-7125
Subject:
Alzheimer disease, Uncaria tomentosa, alkaloids, amyloid, capillary electrophoresis, electrospray ionization mass spectrometry, high performance liquid chromatography, therapeutics, thin layer chromatography
Abstract:
The primary aim of this work was to determine the interactions of an oxindole alkaloid (mitraphylline) isolated from Uncaria tomentosa with β-amyloid 1-40 (Aβ1-40 protein) apply­ing the capillary electrophoresis (CE) method. Specifically the Hummel-Dreyer method and Scatchard analysis were performed to study the binding of oxindole alkaloids with Aβ1-40 protein. Prior to these studies extraction of the alkaloid of interest was carried out. Identifica­tion of the isolated alkaloid was performed by the use of thin-layer chromatography (TLC) and high-performance liquid chromatography (HPLC) combined with electrospray ionization mass spectrometry (ESI-MS). The proposed approach was proved to be an efficient and accurate method for specific compound isolation and identification purposes. Moreover, ana­lytical information from the CE approach can be considered as the valuable tool for binding constant determination. The binding constant of mitraphylline with Aβ1-40 protein deter­mined by the Hummel-Dreyer method and Scatchard analysis equals K = 9.95 x 10⁵ m⁻¹. The results obtained showed the significant binding of the tested compound with Aβ1-40 protein. These results are discussed and interpreted in the view of developing a strategy for identifica­tion of novel compounds of great importance in Alzheimer disease therapy.
Agid:
5230746