Spatial Distribution and Solvent Polarity-Triggered Release of Polypeptide Incorporated into Invertible Micellar Assemblies

Extracting, stabilizing, or delivering biomacromolecules such as proteins and peptides in organic phases have potential applications in biocatalysis, protein extraction, and food antioxidation. However, most current delivery/stabilization platforms face various limitations such as protein/peptide molecular size, platform stability/reusability, and/or potential damage to the cargos. A potential solution to these problems is micellar self-assemblies from amphiphilic invertible polymers (AIPs), which have recently been demonstrated powerful as molecular hosts to deliver both small molecular drugs and functional polypeptides in the aqueous phase. To better understand the function of biomacromoleculea and predict the usefulness of the formed invertible micellar assemblies (IMAs) as biomacromolecular hosts in organic phases, it is critical to characterize the spatial distribution, structure, and dynamics of biomacromolecules in the IMA including upon release. However, the background signals of the IMAs limit th...