Lumbrokinase for degradation and reduction of amyloid fibrils associated with amyloidosis

Abstract

Amyloidosis is a group of diseases caused by the accumulation of insoluble protein aggregates in different parts of the body. Repeated subcutaneous injection of insulin hormones in diabetic patients leads to localized amyloidosis that is found to be cytotoxic. Thus, agents that can dissociate these aggregates are critically needed. In the present study, insulin amyloid dissociation was demonstrated by the treatment of an enzyme lumbrokinase (LK) isolated from earthworm. Thioflavin T (ThT) fluorescence, solution turbidity, particle size analysis, FTIR, CD, atomic force microscopy and cell viability assay were employed to support the dissociation of insulin amyloid in vitro. The small animal optical imaging was used to explore the dissociation of amyloid fibrils in vivo using zebrafish model. The activity of LK towards amyloid dissociation was compared with the standard amyloid fibril degrading agent nattokinase (NK). Our results indicated that LK can be a probable fibril degrading agent for the dissociation of amyloids.