Nanophotonic Approaches for Chirality Sensing.

Chiral nanophotonic materials are promising candidates for biosensing applications because they focus light into nanometer dimensions, increasing their sensitivity to the molecular signatures of their surroundings. Recent advances in nanomaterial-enhanced chirality sensing provide detection limits as low as attomolar concentrations (10-18 M) for biomolecules and are relevant to the pharmaceutical industry, forensic drug testing, and medical applications that require high sensitivity. Here, we review the development of chiral nanomaterials and their application for detecting biomolecules, supramolecular structures, and other environmental stimuli. We discuss superchiral near-field generation in both dielectric and plasmonic metamaterials that are composed of chiral or achiral nanostructure arrays. These materials are also applicable for enhancing chiroptical signals from biomolecules. We review the plasmon-coupled circular dichroism mechanism observed for plasmonic nanoparticles and discuss how hotspot-enhanced plasmon-coupled circular dichroism applies to biosensing. We then review single-particle spectroscopic methods for achieving the ultimate goal of single-molecule chirality sensing. Finally, we discuss future outlooks of nanophotonic chiral systems.

Nanoscale Surface-Induced Unfolding of Single Fibronectin Is Restricted by Serum Albumin Crowding.

Understanding nanoscale protein conformational changes at solid-liquid interfaces is critical for predicting how proteins will impact the performance of biomaterials in vivo. Crowding is an important contributor to conformational stability. Here we apply single-molecule high resolution imaging with photobleaching to directly measure dye-conjugated fibronectin's unfolding in varying conditions of crowding with human serum albumin on aminosilanized glass. Using this approach, we identify serum albumin's crowding mechanism. We find that fibronectin achieves larger degrees of unfolding when not crowded by coadsorbed serum albumin. Serum albumin does not as effectively constrict fibronectin's conformation if it is sequentially, rather than simultaneously, introduced, suggesting that serum albumin's crowding mechanism is dependent on its ability to sterically block fibronectin's unfolding during the process of adsorption. Because fibronectin's conformation is dependent on interfacial macromolecular crowding under in vitro conditions, it is important to consider the role of in vivo crowding on protein activity.