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Substrate Partitioning into Protein Macromolecular Frameworks for Enhanced Catalytic Turnover
Ekaterina Selivanovitch1, Masaki Uchida2, Byeongdu Lee3
1Department of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, Indiana 47405, United States.
ACS Nano
|September 2, 2021
Summary
Scientists created protein macromolecular frameworks (PMFs) using virus-like particles (VLPs) as nanoreactors. These PMFs enhance enzyme catalysis by controlling molecular partitioning, significantly boosting reaction rates for charged substrates.
Area of Science:
- Biochemistry
- Materials Science
- Nanotechnology
Background:
- Biological systems utilize spatial partitioning for efficient enzyme catalysis within cellular compartments.
- Compartmentalization and phase segregation control molecular access and metabolic pathways.
- Nature-inspired designs can mimic these cellular efficiencies.
Purpose of the Study:
- To design virus-like particles (VLPs) as nanoreactor compartments for enzyme sequestration.
- To construct 3D protein macromolecular framework (PMF) materials from these VLPs.
- To investigate the impact of PMF structure on enzyme catalytic activity and molecular partitioning.
Main Methods:
- Virus-like particles (VLPs) were engineered as nanoreactors encapsulating enzyme catalysts.
- 3D protein macromolecular frameworks (PMFs) were assembled from VLPs.
- Small-angle X-ray scattering (SAXS) was used for structural characterization of PMFs.
- Ionic strength was tuned to control molecular partitioning within the charged PMFs.
Main Results:
- PMFs formed a distinct phase in suspension, exhibiting selective partitioning based on molecular charge.
- Positively charged molecules were preferentially incorporated into the PMF, while negatively charged molecules were excluded.
- Enzymes within the PMF showed significantly enhanced catalytic activity for positively charged substrates (8500× faster).
- The catalytic PMF exhibited cooperative behavior with charge-dependent trends distinct from individual nanoreactors.
Conclusions:
- Engineered PMFs serve as effective nanoreactor compartments for enhancing enzyme catalysis.
- Molecular partitioning within PMFs provides a mechanism for fine-tuning reaction rates.
- These biomimetic materials offer a platform for developing advanced catalytic systems.
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