| Autor: |
Kwon S; Department of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States., Andreas MP; Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109, United States., Giessen TW; Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109, United States. |
| Jazyk: |
angličtina |
| Zdroj: |
ACS nano [ACS Nano] 2024 Sep 17; Vol. 18 (37), pp. 25740-25753. Date of Electronic Publication: 2024 Sep 03. |
| DOI: |
10.1021/acsnano.4c08186 |
| Abstrakt: |
Enzyme nanoreactors are nanoscale compartments consisting of encapsulated enzymes and a selectively permeable barrier. Sequestration and colocalization of enzymes can increase catalytic activity, stability, and longevity, highly desirable features for many biotechnological and biomedical applications of enzyme catalysts. One promising strategy to construct enzyme nanoreactors is to repurpose protein nanocages found in nature. However, protein-based enzyme nanoreactors often exhibit decreased catalytic activity, partially caused by a mismatch of protein shell selectivity and the substrate requirements of encapsulated enzymes. No broadly applicable and modular protein-based nanoreactor platform is currently available. Here, we introduce a pore-engineered universal enzyme nanoreactor platform based on encapsulins-microbial self-assembling protein nanocompartments with programmable and selective enzyme packaging capabilities. We structurally characterize our protein shell designs via cryo-electron microscopy and highlight their polymorphic nature. Through fluorescence polarization assays, we show their improved molecular flux behavior and highlight their expanded substrate range via a number of proof-of-concept enzyme nanoreactor designs. This work lays the foundation for utilizing our encapsulin-based nanoreactor platform for diverse future biotechnological and biomedical applications. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
