Electrostatic Self-Assembly of Protein Nanoparticles from Intrinsically Disordered Polypeptide and Globular Protein Pairs.

ABSTRACT: Intracellular delivery of folded, functional proteins remains a critical barrier to realizing the full potential of protein therapeutics. We present a fully aqueous, genetically encoded platform for assembling micellar protein nanoparticles via electrostatic coacervation between anionic globular proteins and multi-domain intrinsically disordered proteins (IDPs) composed of a neutral elastin-like polypeptide (ELP) domain and a cationic disordered histone-derived domain (H5). This biosynthetic system allows modular control over charge density, neutral domain length, and stoichiometry, enabling the formation of homogeneous micellar nanoparticles with high protein payload retention under mild, biologically relevant conditions without organic solvents or covalent modification. Unlike amphiphili

SUBMITTER: Ahn SY 

PROVIDER: S-EPMC12803203 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature