Stability and cytotoxicity of crystallin amyloid nanofibrilsElectronic supplementary information (ESI) available: ThT fluorescence graphs of buffers and solvents used for normalising ThT fluorescence of PNFs in the experiments (Fig. S1 and S2). Representative TEM images of fibrils over a wide range of pH and at variety of temperatures (Fig. S3 and S4). IR spectra of the amide fingerprinting region, including baseline (Fig. S5). See DOI: 10.1039/c4nr04624b

Previous work has identified crystallin proteins extracted from fish eye lenses as a cheap and readily available source for the self-assembly of amyloid nanofibrils. However, before exploring potential applications, the biophysical aspects and safety of this bionanomaterial need to be assessed so as to ensure that it can be effectively and safely used. In this study, crude crystallin amyloid fibrils are shown to be stable across a wide pH range, in a number of industrially relevant solvents, at both low and high temperatures, and in the presence of proteases. Crystallin nanofibrils were compared to well characterised insulin and whey protein fibrils using Thioflavin T assays and TEM imaging. Cell cytotoxicity assays suggest no adverse impact of both mature and fragmented crystallin fibrils on cell viability of Hec-1a endometrial cells. An IR microspectroscopy study supports long-term structural integrity of crystallin nanofibrils. An investigation of the biophysical stability and safety properties of crystallin amyloid nanofibrils - a potential novel bionanomaterial.