Towards gelsolin amyloid formation

Amyloid diseases result from protein misfolding and aggregation into fibrils. Some features of gelsolin amyloidogenic fragments comprised of residues 173-243 (G173-243) and residues 173-202 (G173-202) were investigated by the method of molecular dynamics (MD). The (alpha)-helical structure of G173-243 present in the whole protein unwinds during the course of MD simulation of the fragment G173-243, suggesting that the G173-243 structure is not stable and could unfold before becoming involved in gelsolin amyloid fibril formation. Twelve fragments of G173-202 were used to build a possible (beta)-fibril. During the course of the simulation, G173-202 fragments formed hydrogen bonds and tended to turn by an angle of 10°-20° towards each other.