Proteins are critical components of all cellular and physiological processes. Small alterations in protein activity can make the difference between healthy cells versus cancer, protective immunity versus autoimmune disease, and benign flu versus lethal pandemics. Alterations in activity are often caused by changes in protein structure, which ultimately defines which molecules a protein binds-to or interacts-with, and how strongly it binds to those molecules (binding kinetics).

As an example, just 10 mutations in the spike protein of the SARS-CoV-2 Delta variant compared to the original Wuhan strain resulted in a structural change that enabled the Delta variant to infect individuals at twice the rate and with higher pathogenicity compared to the original strain, leading to hundreds of thousands more deaths. A platform that facilitates the investigation of these protein bindings and measures kinetics in high throughput could thus be immensely useful for studying new variants and predicting the effect of mutations before they occur in the population.

INanoBio’s breakthrough Sensor Integrated Proteome on Chip (SPOC) technology allows researchers to detect interactions and measure binding kinetics of hundreds (later, thousands) of proteins, simultaneously. SPOC is a first-of-its kind technology that expresses hundreds of proteins in situ in nanoscale volume wells and arrays them onto biosensor chips, forgoing the need to pre-purify proteins, and enables immediate kinetic analysis of all arrayed proteins at once.

Researchers can now quickly answer questions such as:
What is the binding specificity of a commercial antibody or an antibody-drug against the target protein (antigen) it was developed against? And does it work against new variants (mutations) of the protein?

Does vaccine-induced antibody immunity work against a new variant of a pathogen (such as SARS-CoV-2)? Is it possible to measure neutralizing antibodies against full proteomes of viruses?

In cancer, how do abnormal mutations or PTMs of onco-proteins change binding to downstream effector proteins, driving disease progression?