Investigation of VDAC1 interaction with small molecules by Differential Scanning Fluorimetry(DSF) (CAT#: STEM-MB-0782-WXH)

Introduction

The voltage-dependent anion channel 1 (VDAC1) is the most abundant protein of the outer mitochondrial membrane (OMM). VDAC1 is responsible of approximatively 90% of the exchanges between the mitochondrion and the cytoplasm regulating the transport of most ions and metabolites of molecular weight less than 5 kDa. In addition, the channel is considered a hub protein interacting with many partners involved in the mitochondrial function including apoptosis. In response to a pro-apoptotic signal, VDAC1 was shown to homo-oligomerize forming a large pore that enables the release of apoptogenic factors from the mitochondrial intermembrane space (IMS) to the cytosol.
Small-molecule ligands specifically interacting with the channel provide an attractive way of exploring its structure-function relationships and can possibly be used as founding stones for future drug-candidates.