Unimer Exchange as a Tool for Programming Enzymatic Degradation through Micellar Dynamics.

ABSTRACT: A key challenge in designing enzyme-responsive micellar nanocarriers lies in balancing their stability and enzymatic degradation. While it has been widely assumed that the micelle-unimer exchange governs enzyme accessibility to the hydrophobic blocks, this relationship had not been directly demonstrated. Here, to uncover this long-assumed mechanistic link, we synthesized a set of triblock amphiphiles that convert by an in situ transition to diblock amphiphiles via reductive cleavage of a central disulfide bond. In parallel, hydrophobicity was independently tuned by modifying the aliphatic end-groups. Enzymatic degradation studies and Förster resonance energy transfer (FRET)-based exchange assays showed two consistent trends across all systems: increasing hydrophobicity led to slower micell

SUBMITTER: Tevet S 

PROVIDER: S-EPMC12606637 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature