STUDY OF OUTWARD SIGNS, MICROSCOPY AND CHEMICAL COMPOSITION OF WALNUT

Objective: Walnut is a medicinal plant that is widely used in traditional medicine. We believe that the study of the medicinal plant material of walnut-fruit in the stage of milky-wax maturity and walnut bark is relevant. We described outward signs and microscopy, the diagnostic features of both whole and grinded raw materials, powder bark of walnut and fruits of walnut in the stage of milky-wax maturity.Methods: Alcohol extraction which was derived from walnut bark is a transparent liquid of brown color and alcohol extraction which was derived walnut fruits in the stage of milky-waxy maturity is a transparent, green-brown liquid with a fragrant smell. We performed thin-layer chromatography for the walnut cortex and identified gallic acid.Results: A method of chromatography-mass spectrometry in alcohol extraction from walnut fruit in the stage of milky-waxy maturity allowed to identify 17 compounds belonging to different classes of biologically active substances. We identified sugars, flavonoids, phenolic compounds of coumarins and organic acids. In alcohol extraction from the walnut bark we identified marker substances

Synthetic Fragments of Receptor for Advanced Glycation End Products Bind Beta-Amyloid 1-40 and Protect Primary Brain Cells From Beta-Amyloid Toxicity

Receptor for advanced glycation end products (RAGE) is involved in the pathogenesis of Alzheimer’s disease. We have previously revealed that RAGE fragment sequence (60–76) and its shortened analogs sequence (60–70) and (60–65) under intranasal insertion were able to restore memory and improve morphological and biochemical state of neurons in the brain of bulbectomized mice developing major AD features. In the current study, we have investigated the ability of RAGE peptide (60–76) and five shortened analogs to bind beta-amyloid (Aβ) 1–40 in an fluorescent titration test and show that all the RAGE fragments apart from one [sequence (65–76)] were able to bind Aβ in vitro. Moreover, we show that all RAGE fragments apart from the shortest one (60–62), were able to protect neuronal primary cultures from amyloid toxicity, by preventing the caspase 3 activation induced by Aβ 1–42. We have compared the data obtained in the present research with the previously published data in the animal model of AD, and offer a probable mechanism of neuroprotection of the RAGE peptide