Journal of Proteomics & Bioinformatics
Open Access
ISSN: 0974-276X
ISSN: 0974-276X
Muhammad Ehsan and Pil Seok Chae
Hanyang University, South Korea
Posters & Accepted Abstracts: J Proteomics Bioinform
Biological membranes contain a variety of membrane proteins that act as receptors, signal transducers, channels, transporters, motors and anchors. High resolution structures of membrane proteins are of paramount importance for understanding mechanism of action at a molecular level and are of significant implications for biomedical and pharmaceutical applications. Detergents, amphipathic molecules, serve as indispensable tools for extracting membrane proteins from the membranes and maintaining them in a soluble and active state, which is essential for successful downstream characterizations. However, membrane proteins in a conventional detergent tend to aggregate and denature over time. To resolve an issue associated with membrane protein stability, we developed steroidal amphiphiles with a penta-saccharide head group. When these agents were evaluated for the ability to stabilize a diverse range of membrane proteins, some representatives conferred marked stability to membrane proteins tested here compared to a conventional detergent.