Role of α-Crystallin protein-protein interactions in disorders of the system and its therapeutic approaches: a new study

Abstract

α- Crystallin, a major eye lens protein with chaperone activity is vital in cataract development. As a member of the small heat shock protein superfamily, α-Crystallin is able to recognise and bind denatured or unfolded proteins, thereby preventing their aggregation. An important constituent of eye drops and artificial tears is polyethylene glycol-400(PEG-400) which can interact with α- Crystallin and lead to alterations in its tertiary structure, namely the global transition to a non-native form. Another protein, which is characterised by its presence in the insoluble fraction of vertebrate nuclear fiber cells, is Galectin-Related Interfiber Protein (GRIFIN) in the Ocular lens which is a novel binding partner of α-Crystallin. Formation of complexes involving such proteins may influence cell elongation and suture formation during lens development. The binding of PEG-400 or GRIFIN with α-Crystallin may serve as a rationale for the discovery of various therapeutic molecules used for the treatment of eye-related diseases involving crystallin proteins.