Towards gelsolin amyloid formation
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Updated: Aug 21, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Inta Liepina1, Paul Janmey, Cezary Czaplewski
1Latvian Institute of Organic Synthesis, Aizkraukles str. 21, Riga, LV1006, Latvia. inta@osi.lv
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 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 degrees -20 degrees towards each other.
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