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pH Induced Conformational Transitions in the Transforming Growth Factor β-Induced Protein (TGFβIp) Associated Corneal Dystrophy Mutants.

Sci Rep. 2016; 
MuruganElavazhagan,VenkatramanAnandalakshmi,LeiZhou,MouvetVictoria,Rui Yi LimRayne,MurugananthamNandhakumar,GohEunice,Swee Lim PehGary,BeuermanRoger W,ChaurasiaShyam S,RajamaniLakshminarayanan,MehtaJodhb
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Custom Vector Construction The cDNA constructs of the 4th_FAS1 domains of the WT TGFβIp, the mutants R555W and H572R were bought from Genscript (Piscataway, NJ) in pUC57 vectors. Get A Quote

摘要

Most stromal corneal dystrophies are associated with aggregation and deposition of the mutated transforming growth factor-β induced protein (TGFβIp). The 4(th)_FAS1 domain of TGFβIp harbors ~80% of the mutations that forms amyloidogenic and non-amyloidogenic aggregates. To understand the mechanism of aggregation and the differences between the amyloidogenic and non-amyloidogenic phenotypes, we expressed the 4(th)_FAS1 domains of TGFβIp carrying the mutations R555W (non-amyloidogenic) and H572R (amyloidogenic) along with the wild-type (WT). R555W was more susceptible to acidic pH compared to H572R and displayed varying chemical stabilities with decreasing pH. Thermal denaturation studies at acidic pH showe... More

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