Abstract by Hsien-Jung Lavender Lin

Personal Infomation

Presenter's Name

Hsien-Jung Lavender Lin

Degree Level



Stella Park
Nathan Zuniga
John Price

Abstract Infomation


Chemistry and Biochemistry

Faculty Advisor

J.C. Price


Quantifying Proteostasis: An In Vivo Protein Quality Assay Based On Fold Stability


Aging is one of the primary risk factors of many diseases. A well accepted explanation of aging is decline in proteostasis, a functional balance between protein synthesis, folding, degradation, localization, and modification. We had developed a protein fold assay that measures in vivo protein stability (DGfolding) to access the quality of protein, a component of proteostasis, at the proteome level. Here we present the application of the protein quality assay on human cardiac amyloidosis. Transthyretin (TTR) amyloid is responsible for the disease. Different concentration of TTR stabilizer, Diflunisal, is used on control and diseased human serum to learn how protein folding stability of TTR and other protein react to the treatment and the protein quality control change with the disease.  The result of this study validates the protein quality assay, which can be used in the Kinetic Proteostasis model for aging study. Furthermore, it establishes a baseline for future study in treatment effectiveness and early biomarker identification for cardiac amyloidosis.