Ligand Binding-Induced Cellular Membrane Deformation is Correlated with the Changes in Membrane Stiffness.

Study interaction between ligands and protein receptors is a key step for biomarker research and drug discovery. In situ measurement of cell surface membrane protein binding on whole cells eliminates the cost and pitfalls associated with membrane protein purification. Ligand binding to membrane protein was recently found to induce nanometer-scale cell membrane deformations, which can be monitored with real-time optical imaging to quantify ligand/protein binding kinetics.

Label-free imaging and biomarker analysis of exosomes with plasmonic scattering microscopy.

Exosome analysis is a promising tool for clinical and biological research applications. However, detection and biomarker quantification of exosomes is technically challenging because they are small and highly heterogeneous. Here, we report an optical approach for imaging exosomes and quantifying their protein markers without labels using plasmonic scattering microscopy (PSM).

In Situ Analysis of Membrane-Protein Binding Kinetics and Cell-Surface Adhesion Using Plasmonic Scattering Microscopy.

Surface plasmon resonance microscopy (SPRM) is an excellent platform for in situ studying cell-substrate interactions. However, SPRM suffers from poor spatial resolution and small field of view. Herein, we demonstrate plasmonic scattering microscopy (PSM) by adding a dry objective on a popular prism-coupled surface plasmon resonance (SPR) system.

Label-Free Imaging of Single Proteins and Binding Kinetics Using Total Internal Reflection-Based Evanescent Scattering Microscopy.

Single-molecule detection can push beyond ensemble averages and reveal the statistical distributions of molecular properties. Measuring the binding kinetics of single proteins also represents one of the critical and challenging tasks in protein analysis. Here, we report total internal reflection-based evanescent scattering microscopy with label-free single-protein detection capability.

Molecularly resolved, label-free nucleic acid sensing at solid-liquid interface using non-ionic DNA analogues.

Nucleic acid-based biosensors, where the capture probe is a nucleic acid, , DNA or its synthetic analogue xeno nucleic acid (XNA), offer interesting ways of eliciting clinically relevant information from hybridization/dehybridization signals. In this respect, the application of XNA probes is attractive since the drawbacks of DNA probes might be overcome. Within the XNA probe repertoire, peptide nucleic acid (PNA) and morpholino (MO) are promising since their backbones are non-ionic.

How stable are the collagen and ferritin proteins for application in bioelectronics?

One major obstacle in development of biomolecular electronics is the loss of function of biomolecules upon their surface-integration and storage. Although a number of reports on solid-state electron transport capacity of proteins have been made, no study on whether their functional integrity is preserved upon surface-confinement and storage over a long period of time (few months) has been reported. We have investigated two specific cases-collagen and ferritin proteins, since these proteins exhibit considerable potential as bioelectronic materials as we reported earlier.

Nanoscale On-Silico Electron Transport via Ferritins.

Silicon is a solid-state semiconducting material that has long been recognized as a technologically useful one, especially in electronics industry. However, its application in the next-generation metalloprotein-based electronics approaches has been limited. In this work, the applicability of silicon as a solid support for anchoring the iron-storage protein ferritin, which has a semiconducting iron nanocore, and probing electron transport via the ferritin molecules trapped between silicon substrate and a conductive scanning probe has been investigated.