Denaturation and solvent effect on the conformation and fibril formation of TGFBIp.

ABSTRACT:

Purpose

Transforming growth factor beta-induced protein (TGFBIp) aggregates into the phenotypic amyloid fibrils and/or non-amyloid deposits in corneal dystrophies and other disorders. While significant progress has been made in molecular genetics to successfully establish the link between the missense mutations of TGFBI and TGFBIp-related corneal dystrophies, the underlying mechanism for the abnormal aggregation remains elusive due to the lack of insights into the conformational perturbations induced by mutations. In the present study, we examined the effects of denaturants and a co-solvent on recombinant TGFBIp, with a focus on protein conformational changes and amyloid fibril formation.

Methods

Recombinant TGFBIp was subjected to various spectroscopic studies, such as far-

SUBMITTER: Grothe HL 

PROVIDER: S-EPMC2790481 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature