m Ghaffari Sharaf - Department of Chemical and Materials Engineering, University of Alberta, Edmonton, AB, Canada.Ingenuity Lab, University of Alberta, Edmonton, AB, Canada.
s Cetinel - Department of Chemical and Materials Engineering, University of Alberta, Edmonton, AB, Canada.Ingenuity Lab, University of Alberta, Edmonton, AB, Canada.
v Semenchenko - National Institute of Nanotechnology, National Research Council, Edmonton, AB, Canada.
l Unsworth - Department of Chemical and Materials Engineering, University of Alberta, Edmonton, AB, Canada.National Institute of Nanotechnology, National Research Council, Edmonton, AB, Canada.

Crystallins are main proteins of the eye lens. Aggregation of lens proteins into insoluble fibrillar structures is believed to be the main reason of cataracts. Today the only effective treatment for cataract is surgery and it is not accessible for all people especially in developing world. It is thought that specific targeting of these fibrillar aggregates could help to development of novel approaches for cataract treatment. βB2-crystallin, one of the main proteins of lens crystallin proteins, was used to form model fibrillar aggregates in vitro. Phage display technique was used to identify peptides that bound to βB2-crystallin fibrils with high affinity. Recombinantly expressed βB2-crystallin was fibrillated in 10% (v/v) trifluoroethanol (TFE) solution. Thioflavin-T (ThT) assay and transmission electron microscopy (TEM) were used to confirm the fibrillation of βB2-crystallin. Specific targeting of identified peptides was analyzed using enzyme-linked immunosorbent assay (ELISA) and competitive inhibition assay.

Phage display, βB2-crystallin, fibrillar aggregate, cataract, targeting peptide