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 degrees -20 degrees towards each other.
Liepina
Inta
I
Latvian Institute of Organic Synthesis, Aizkraukles str. 21, Riga, LV1006, Latvia. inta@osi.lv
Janmey
Paul
P
Czaplewski
Cezary
C
Liwo
Adam
A
D000682:Amyloid / Q000737:chemistry*; D000686:Amyloidosis / Q000209:etiology / Q000378:metabolism; D018260:Gelsolin / Q000737:chemistry*; D006801:Humans; D066298:In Vitro Techniques; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D013816:Thermodynamics
D000682:Amyloid; D018260:Gelsolin; D010446:Peptide Fragments