Investigating the influences of redox buffer compositions on the amyloid fibrillogenesis of hen egg-white lysozyme

Cysteine inhibits amyloid fibrillation of lysozyme and directs the formation of small worm‐like aggregates through non‐covalent interactions

“…Interestingly, Cys directed the formation of small worm‐like aggregates in the unfolded lysozyme. The effect of Cys was non‐covalent, suggesting that the novel inhibitory mechanism through “thiophilic interaction,” which is different from those previously reported through the reduction of disulfide bridges …”

“…As shown in the above experiments, Cys inhibits amyloid aggregation of HEWL and directs the formation of small worm‐like aggregates of the unfolded HEWL. Notably, the amyloid aggregation of HEWL is inhibited by chemically modifying the residues and disrupting the disulfide bonds . Thus, we investigated if Cys forms covalent modifications on HEWL in solution at pH 2.…”

Biophysical insight into the anti-amyloidogenic behavior of taurine

“…The excitation and emission slit widths were set at 10 nm. All data are fitted by using following equation in Sigma plot [26].…”

Quinopeptide formation associated with the disruptive effect of epigallocatechin-gallate on lysozyme fibrils

“…During amyloid formation, the disulfide bonds in lysozyme become more accessible to the solvent [19] and free thiols may be produced due to disulfide breakage, particularly in the presence of thiol-reacting reagents or reducing compounds [44][45][46]. In another experiment, the production of free thiols in the process of lysozyme fibrillation was confirmed by the Ellman method [47].…”