Isolation of amyloid by solubilization in water.

Amyloid fibrils are highly insoluble in neutral aqueous media of regular ionic strengths making solubilization a difficult task that normally calls for extremely harsh treatment. This is among the reasons for the routine employment of synthetic proteins in amyloid research, where the amylogenic components are needed. Here we describe a process for solubilizing amyloid in pure water that we adopted from a method developed by Mordechai Pras and associates. We have used it for solubilizing cystatin C amyloid and extracting it out of leptomeningeal tissue and skin from Hereditary Cerebral Hemorrhage with Amyloidosis-Icelandic type (HCHWA-I) patients. HCHWA-I is a rare and very aggressive heritable form of cerebral amyloid angiopathy (CAA)-specific Icelandic type. Similar approach has been employed for solubilization of different forms of amyloid from other organs suggesting broad range of applicability.