Biomolecular ligands as tools to modulate the optical and chiroptical properties of gold nanoclusters.

Biomolecule-stabilized gold nanoclusters (AuNCs) have become functional nanomaterials of interest because of their unique optical properties, together with excellent biocompatibility and stability under biological conditions. In this review, we explore the recent advancements in the application of biomolecular ligands for synthesizing AuNCs. Various synthesis approaches that are employing amino acids, peptides, proteins, and DNA as biomolecular scaffolds are reviewed.

Engineering Protein-Nanoparticle Hybrids as Targeted Contrast Agents.

Iron oxide nanoparticles (IONPs) have shown great promise in biomedical applications, particularly as MRI contrast agents due to their magnetic properties and biocompatibility. Although several IONPs have been approved by regulatory agencies as MRI contrast agents, their primary application as negative contrast agents limits their usage. Additionally, there is an emerging need for the development of molecular contrast agents that can specifically target biomarkers, enabling more accurate and sensitive diagnostics.

Thickness Determination and Control in Protein-Based Biomaterial Thin Films.

Controlling the thickness and uniformity of biomaterial films is crucial for their application in various fields including sensing and bioelectronics. In this work, we investigated film assemblies of an engineered repeat protein─specifically, the consensus tetratricopeptide repeat (CTPR) protein ─a system with unique robustness and tunability. We propose the use of microreflectance spectroscopy and apparent color inspection for the quick assessment of the thickness and uniformity of protein-based biomaterial films deposited on oxidized silicon substrates.

The strongest protein binder is surprisingly labile.

Bacterial adhesins are cell-surface proteins that anchor to the cell wall of the host. The first stage of infection involves the specific attachment to fibrinogen (Fg), a protein found in human blood. This attachment allows bacteria to colonize tissues causing diseases such as endocarditis.

Engineering bio-brick protein scaffolds for organizing enzyme assemblies.

Enzyme scaffolding is an emerging approach for enhancing the catalytic efficiency of multi-enzymatic cascades by controlling their spatial organization and stoichiometry. This study introduces a novel family of engineered SCAffolding Bricks, named SCABs, utilizing the consensus tetratricopeptide repeat (CTPR) domain for organized multi-enzyme systems. Two SCAB systems are developed, one employing head-to-tail interactions with reversible covalent disulfide bonds, the other relying on non-covalent metal-driven assembly via engineered metal coordinating interfaces.