Analysis of Hsp60 inhibitors by Differential Scanning Fluorimetry(DSF) (CAT#: STEM-MB-0780-WXH)

Introduction

Heat shock protein 60 (Hsp60) is a barrel-shaped, molecular chaperone that promotes protein folding in the mitochondria and it has been implicated as a potential target in cancer and neurodegenerative diseases. Early efforts towards Hsp60 inhibitors have focused on its ATPase activity or ability to refold damaged proteins. However, Hsp60 is only active when it assembles into oligomers, so inhibiting PPIs is another possible way to interrupt its function. Each Hsp60 monomer is composed of an apical, intermediate and equatorial domain. Inter-protomer contacts involving the apical and equatorial domains hold together the homo-heptameric rings. This architecture allows unfolded proteins to enter the heptamer’s central cavity, where they are folded in the interior chamber.