Quantitative Characterization of Partitioning Stringency in SELEX.

Maintaining stringent conditions in SELEX (Systematic Evolution of Ligands by EXponential enrichment) is crucial for obtaining high-affinity aptamers. However, excessive stringency greatly increases the risk of SELEX failure. Controlling stringency has remained a technical challenge, largely dependent on intuition, due to the absence of a clear, quantitative measure of stringency.

Integrating advanced Microfluidic lateral flow systems with a finger-prick blood collection cartridge to create an all-in-one platform for point-of-care diagnostics.

Rapid, point-of-care tests are critical for early diagnosis of disease and detection of biological threats. Lateral flow immunoassays (LFIAs) are well-suited for point-of-care testing due to their ease of use and straightforward readout. However, limitations in sensitivity, quantification, and integration into sample-to-result systems indicate the need for further advancements.

Maximizing the Accuracy of Equilibrium Dissociation Constants for Affinity Complexes: From Theory to Practical Recommendations.

The equilibrium dissociation constant () is a major characteristic of affinity complexes and one of the most frequently determined physicochemical parameters. Despite its significance, the values of obtained for the same complex under similar conditions often exhibit considerable discrepancies and sometimes vary by orders of magnitude. These inconsistencies highlight the susceptibility of determination to large systematic errors, even when random errors are small.

FRET Assays for the Identification of HSP90-Sba1 and HSP90α-p23 Binding Inhibitors.

Heat shock protein 90 (HSP90) is a critical target for anticancer and anti-fungal-infection therapies due to its central role as a molecular chaperone involved in protein folding and activation. In this study, we developed Förster Resonance Energy Transfer (FRET) assays to characterize the binding of HSP90 to its co-chaperone Sba1, as well as that of the homologous HSP90α to p23. The assay for HSP90α binding to p23 enables selectivity assessment for compounds aimed to inhibit the binding of HSP90 to Sba1 without affecting the physiological activity of HSP90α.