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TitleStability and cytotoxicity of crystallin amyloid nanofibrils
Publication TypeJournal Article
Year of Publication2014
AuthorsKaur, M., Healy J., Vasudevamurthy M., Lassé M., Puskar L., Tobin M.J., Valéry C., Gerrard J.A., and Sasso L.
Pagination13169 - 13178
Date Published2014
ISSN20403364 (ISSN)
Keywordscrystallin, Nano-fibrils
AbstractPrevious 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. © 2014 the Partner Organisations.

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