Fusing fluorescent proteins and ferritin for protein cage based lighting devices

Area of Science:

• Biotechnology
• Materials Science
• Optoelectronics

Background:

• Ferritin cages stabilize active cargoes and are explored for bio-hybrid light-emitting diodes (Bio-HLEDs).
• Current methods for integrating fluorescent proteins into ferritin cages compromise protein functionality and stability.

Purpose of the Study:

• To develop a novel fusion protein combining Thermotoga maritima apoferritin (TmaFt) and mGreenlantern (mGL) to overcome limitations in Bio-HLED development.
• To optimize the fusion protein (mGL-TmaFt) for enhanced stability and photophysical properties.

Main Methods:

• Constructed a fusion protein (mGL-TmaFt) linking mGreenlantern (mGL) and Thermotoga maritima apoferritin (TmaFt).
• Optimized linker length, assembly efficiency, and cargo loading (mGL@TmaFt).
• Evaluated thermal and structural stability in solution and polymer matrices.

Main Results:

• The mGL-TmaFt fusion protein demonstrated enhanced thermal and structural stability.
• Encapsulation within ferritin cages (mGL@TmaFt) reduced chromophore deactivation and heat transfer.
• Bio-HLEDs incorporating mGL@TmaFt showed significantly improved device stability (30- and 15-fold higher).

Conclusions:

• Protein cage design offers a promising strategy for photon manipulation in lighting devices.
• The developed fusion protein enhances stability and performance of Bio-HLEDs.
• This approach provides a robust platform for advanced bio-hybrid optoelectronic applications.