Reaction of 2-Propynyl Acetate and 1,1-dimethyl-2-propynyl Chloroacetate with Amines

Russian Journal of General Chemistry -     

Molecular Mechanisms of Amylin Turnover,Misfolding and Toxicity in the Pancreas

Amyloidosis is a common pathological event in which proteins self-assemble into misfolded soluble and insoluble molecular forms, oligomers and fibrils that are often toxic to cells. Notably, aggregation-prone human islet amyloid polypeptide (hIAPP), or amylin, is a pancreatic hormone linked to islet β-cells demise in diabetics. The unifying mechanism by which amyloid proteins, including hIAPP, aggregate and kill cells is still matter of debate. The pathology of type-2 diabetes mellitus (T2DM) is characterized by extracellular and intracellular accumulation of toxic hIAPP species, soluble oligomers and insoluble fibrils in pancreatic human islets, eventually leading to loss of β-cell mass. This review focuses on molecular, biochemical and cell-biology studies exploring molecular mechanisms of hIAPP synthesis, trafficking and degradation in the pancreas. In addition to hIAPP turnover, the dynamics and the mechanisms of IAPP–membrane interactions; hIAPP aggregation and toxicity in vitro and in situ; and the regulatory role of diabetic factors, such as lipids and cholesterol, in these processes are also discussed.     

Composite supports based on bentonite clay and polysaccharides

Fundamental aspects of the interaction between the bentonite clay and self-structuring polysaccharides, agar-agar and sodium salt of carboxymethyl cellulose, were studied. The possibility of using the resulting composite gels as drug carriers was examined.