Fusing fluorescent proteins and ferritin for protein cage based lighting devices.

Authors

Alba Sanz-Velasco, Marta Patrian, Mattia Nieddu, Boxuan Shen, Juan Pablo Fuenzalida Werner, Mauri A Kostiainen, Rubén D Costa, Eduardo Anaya-Plaza

Published in

Nanoscale. Apr 04, 2025. Epub Apr 04, 2025.

Abstract

Ferritin cages are an effective platform to encapsulate and stabilize a range of active cargoes and present a promising stepping stone towards a wide range of applications. They have been explored for optoelectronic applications in combination with fluorescent proteins towards bio-hybrid light-emitting diodes (Bio-HLEDs) only recently. However, protein integration within the cage or coassembled ferritin cages relies on electrostatic interactions and requires the supercharging of the fluorescent protein that easily compromises functionality and stability. To address this limitation, we have developed a fusion protein combining the Thermotoga maritima apoferritin (TmaFt) with a green fluorescent protein named mGreenlantern (mGL). This approach avoids jeopardizing both the cage assembly capability of TmaFt and the photophysical features of mGL. After optimizing the fusion protein mGL-TmaFt with respect to the linker length, assembling efficiency, and mGL payload into the cage (mGL@TmaFt), our findings reveal that they exhibited enhanced thermal and structural stabilities in both solution and when embedded into a polymer matrix. This enables effective mGL shielding, reducing H-transfer deactivation of the chromophore and water-assisted heat transfer across the polymer network. Indeed, the photo-induced heat generation in Bio-HLEDs operating at high currents was significantly reduced, resulting in a 30- and 15-fold higher device stability compared to references with either mGL or mGL-TmaFt proteins, respectively. Overall, this work sets in the potential of protein cage design for photon manipulation in protein lighting devices.

PMID:
40184033
Bibliographic data and abstract were imported from PubMed on 04 Apr 2025.

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