Recombinant protein platform for high-throughput investigation of peptide-liposome interactions via fluorescence anisotropy depolarization.

ABSTRACT: Many cytosolic proteins critical to membrane trafficking and function contain an unstructured domain that can bind to specific membranes, with a transition into an amphipathic helix induced upon membrane association. These inducible amphipathic helices often play a critical role in organelle recognition and subsequent function by these cytosolic proteins, but the tools and techniques used to characterize affinity towards specific membranes are low-throughput and highly dependent on the solubility of the inducible amphipathic helix. Here, we introduce a modular recombinant protein platform for rapidly measuring the binding affinity of inducible amphipathic helices towards a variety of membrane compositions and curvatures using high-throughput fluorescence anisotropy measurements. Inducible

SUBMITTER: Margaritakis A 

PROVIDER: S-EPMC12132265 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature