Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents.

ABSTRACT: Methods for maintaining membrane proteins in their native state after removal from the lipid bilayer are essential for the study of this important class of biomacromolecules. Common solubilization strategies range from the use of detergents to more complex systems that involve a polypeptide working in concert with lipids or detergents, such as nanodiscs, picodiscs, and peptidiscs, in which an engineered protein or synthetic peptide surrounds the membrane protein along with a lipid sheath. Picodiscs employ the protein saposin A, which naturally functions to facilitate lipid degradation in the lysozome. Saposin A-amphiphile complexes therefore tend to be most stable at acidic pH, which is not optimal for most membrane protein applications. In search of new picodisc assemblies, we have explor

SUBMITTER: Kurgan KW 

PROVIDER: S-EPMC8044043 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature