Towards gelsolin amyloid formation

Abstract

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 α-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 β-fibril. During the course of the simulation, G173-202 fragments formed hydrogen bonds and tended to turn by an angle of 10deg;-20° towards each other. © 2004 Wiley Periodicals, Inc.