Effects of the H6R and D7H Mutations on the Heparin-Dependent Modulation of Zinc-Induced Aggregation of Amyloid β

Molecular Biology - Zinc ions and glycosaminoglycans (GAGs) are found in amyloid deposits and are known to modulate the β-amyloid peptide (Аβ) aggregation, which is thought to be a...     

Patterns of Reproduction of Pontocaspian Relict Paramysis lacustris within Distribution Area

Reproduction has been studied of Paramysis lacustris, pontocaspian relict, in the centre of its natural area, and in southern and northern zones of acclimatisation. Life cycles of the animals are identical in the distribution area. The effect of female size on fecundity is only slightly expressed within each generation. Significant correlations of these indices were obtained in seasonal aspect. Specific fecundity is represented by maximum values in the centre of the area and declines in the north-western direction of introduction. The relation of fecundity to egg weight reflecting correlation of K-r reproduction strategy is reduced in the regions of introduction. Reproduction effort, i.e. ratio of eggs weight to female weight, is the most stable index within the distribution area. Cumulative potential growth, including soma as well as generative products, was nearer in spite of considerable temperature difference in animal growth.     

Zinc-induced interactions of the metal-binding domain of beta-amyloid with nucleic acids and glycosaminoglycans

Zinc ions form complexes with β-amyloid peptides and play an important role in Alzheimer’s disease pathogenesis. It has been demonstrated by turbidimetry and correlation spectroscopy that synthetic peptide Aβ16 representing the metal-binding domain of β-amyloid is able to interact with nucleic acids, chondroitin polysulfate, and dextran sulfates in the presence of zinc ions. The amino acid D7H substitution enhanced the peptide binding to polyanions, whereas the H6R and H6A-H13A substitutions abolished this interaction. It is suggested that the metal-binding domain may serve as a zinc-dependent site of β-amyloid interaction with biological polyanions including DNA, RNA, and glycosaminoglycans.