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SpyTag-Embedded Protein Nanoparticles Enable pH-Dependent Protein Loading
Nevin Jaison1, Richard Duff1, Kavita Yadav2
1School of Human Sciences, University of Derby, Derby, UK.
Molecular Biotechnology
|August 8, 2026
Summary
Researchers developed stable, bioactive protein nanoparticles (NPs) using Bacillus thuringiensis scaffolds. These customizable NPs show potential for targeted drug delivery, especially in acidic tumor environments, due to their pH-responsive binding capabilities.
Area of Science:
- Biomaterials Science
- Nanotechnology
- Protein Engineering
Background:
- Functional protein particles are versatile biomaterials for nano-designs, drug delivery, and biocatalysis.
- Challenges in assembling protein nanostructures include complex interactions and variable surface charges.
- Genetic modularity and nanoscale engineering enable customizable protein systems.
Purpose of the Study:
- To present a modular strategy for assembling bioactive protein nanoparticles (NPs).
- To engineer stable and functional protein NPs using Bacillus thuringiensis scaffolds.
- To explore the potential of these NPs for targeted therapeutic delivery.
Main Methods:
- Genetically fusing the Cry1Ac scaffold with monomeric red fluorescent protein or SpyTag002.
- Utilizing the SpyTag/SpyCatcher system for modular protein recruitment onto NP surfaces.
- Assessing NP structural integrity, fluorescence stability, and pH-dependent binding properties.
Main Results:
- Generated stable, bioactive protein NPs with maintained structural integrity and fluorescence.
- Demonstrated modular protein loading via the SpyTag/SpyCatcher system.
- Confirmed pH-responsive binding of SpyTag-embedded NPs to SpyCatcher.
Conclusions:
- The developed protein NPs are stable, bioactive, and customizable.
- The SpyTag/SpyCatcher system enables efficient and targeted functionalization.
- The pH sensitivity and stability make these NPs promising for therapeutic delivery in acidic environments like tumors.
