Acetic Acid Enables Precise Tailoring of the Mechanical Behavior of Protein-Based Hydrogels.

Engineering viscoelastic and biocompatible materials with tailored mechanical and microstructure properties capable of mimicking the biological stiffness (<17 kPa) or serving as bioimplants will bring protein-based hydrogels to the forefront in the biomaterials field. Here, we introduce a method that uses different concentrations of acetic acid (AA) to control the covalent tyrosine-tyrosine cross-linking interactions at the nanoscale level during protein-based hydrogel synthesis and manipulates their mechanical and microstructure properties without affecting protein concentration and (un)folding nanomechanics. We demonstrated this approach by adding AA as a precursor to the preparation buffer of a photoactivated protein-based hydrogel mixture. This strategy allowed us to synthesize hydrogels made from bovine serum albumin (BSA) and eight repeats protein L structure, with a fine-tailored wide range of stiffness (2-35 kPa). Together with protein engineering technologies, this method will open new routes in developing and investigating tunable protein-based hydrogels and extend their application toward new horizons.

Toward Tunable Protein-Driven Hydrogel Lens.

Despite the significant progress in protein-based materials, creating a tunable protein-activated hydrogel lens remains an elusive goal. This study leverages the synergistic relationship between protein structural dynamics and polymer hydrogel engineering to introduce a highly transparent protein-polymer actuator. By incorporating bovine serum albumin into polyethyleneglycol diacrylate hydrogels, the authors achieved enhanced light transmittance and conferred actuating capabilities to the hydrogel. Taking advantage of these features, a bilayer protein-driven hydrogel lens that dynamically modifies its focal length in response to pH changes, mimicking the adaptability of the human lens, is fabricated. The lens demonstrates durability and reproducibility, highlighting its potential for repetitive applications. This integration of protein-diverse biochemistry, folding nanomechanics, and polymer engineering opens up new avenues for harnessing the wide range of proteins to potentially propel various fields such as diagnostics, lab-on-chip, and deep-tissue bio-optics, advancing the understanding of incorporating biomaterials in the optical field.

Collective Rayleigh Scattering from Molecular Ensembles under Strong Coupling.

Rayleigh scattering is usually considered to be the elastic scattering of photons from subwavelength physical objects, such as small particles or molecules. Here, we present a quantitative spectroscopic study of the scattering properties of molecules embedded in an optical cavity under strong coupling conditions, where the collective interaction between the molecules and the cavity gives rise to composite light-matter excitations known as cavity polaritons. We show that the polaritonic states exhibit strong resonant Rayleigh scattering, which depends on both the coupling strength and detuning and reaching ∼25% efficiency. Since the polaritonic wave functions in such systems are delocalized, our observations correspond to the collective scattering of each photon from a large ensemble of molecules.