Simple Sol‐Gel Protein Stabilization toward Rainbow and White Lighting Devices

Abstract

Fluorescent proteins (FPs) are heralded as a paradigm of sustainable materials for photonics/optoelectronics. However, their stabilization under non‐physiological environments and/or harsh operation conditions is the major challenge. Among the FP‐stabilization methods, classical sol‐gel is the most effective, but less versatile, as most of the proteins/enzymes easily degraded due to the need of multi‐step processes, surfactants, and mixed water/organic solvents in extreme pH. Herein, we revisited sol‐gel chemistry with archetypal FPs (mGL; mCherry), simplifying the method by one‐pot, surfactant‐free, and aqueous media (phosphate buffer saline pH = 7.4). The synthesis mechanism involves the direct reaction of the carboxylic groups at the FP surface with the silica precursor, generating a positively charged FP intermediate that acts as a seed for the formation of size‐controlled mesoporous FP@SiO2 nanoparticles. Green‐/red‐emissive (single‐FP component) and dual‐emissive (multi‐FPs component; no need of kinetic studies) FP@SiO2 were prepared without affecting the FP photoluminescence and stabilities (>6 months) under dry storage and organic solvent suspensions. Finally, FP@SiO2 color filters were applied to rainbow and white bio‐hybrid light‐emitting diodes featuring up to 15‐fold enhanced stabilities without reducing luminous efficacy compared to references with native FPs. Overall, we demonstrate an easy, versatile, and effective FP‐stabilization method in FP@SiO2 towards sustainable protein lighting.This article is protected by copyright. All rights reserved