Study of cosolvent-induced alpha-chymotrypsin fibrillogenesis: does protein surface hydrophobicity trigger early stages of aggregation reaction?
The misfolding of specific proteins is often associated with their assembly into fibrillar aggregates, commonly termed amyloid fibrils. Despite the many efforts expended to characterize amyloid formation in vitro, there is no deep knowledge about the environment (in which aggregation occurs) as well as mechanism of this type of protein aggregation. Alpha-chymotrypsin was recently driven toward amyloid aggregation by the addition of intermediate concentrations of trifluoroethanol. In the present study, approaches such as turbidimetric, thermodynamic, intrinsic fluorescence and quenching studies as well as chemical modification have been successfully used to elucidate the underlying role of hydrophobic interactions (involved in early stages of amyloid formation) in alpha-chymotrypsin-based experimental system.
Khodarahmi
Reza
R
Department of Pharmacognosy and Biotechnology, Faculty of Pharmacy, Kermanshah University of Medical Sciences, P. O. Box 67145-1673, Kermanshah, Iran. rkhodarahmi@mbrc.ac.ir
Soori
Hosnieh
H
Amani
Mojtaba
M
D000682:Amyloid / Q000737:chemistry*; D002918:Chymotrypsin / Q000737:chemistry* / Q000187:drug effects; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D055503:Protein Multimerization / Q000187:drug effects; D012997:Solvents / Q000494:pharmacology*; D014270:Trifluoroethanol / Q000494:pharmacology
D000682:Amyloid; D012997:Solvents; D014270:Trifluoroethanol; D002918:Chymotrypsin; C117608:alpha-chymotrypsin