The equilibrium dissociation constant (K d) is a major characteristic of affinity complexes and
one of the most frequently determined physicochemical parameters. Despite its significance …

Molecular interactions play a vital role in regulating various physiological and biochemical
processes in vivo. Kinetic capillary electrophoresis (KCE) is an analytical platform that offers …

Herein, we report for the first time the isolation of DNA aptamers directed against the whole
tau protein, an important Alzheimer's disease (AD) biomarker. Non-SELEX approach based …

Selection of oligonucleotide aptamers involves consecutive rounds of affinity isolation of
target-binding oligonucleotides from a random-sequence oligonucleotide library. Every next …

The limit-of-detection (LOD) in analytical instruments with fluorescence detection can be
improved by reducing noise of optical background. Efficiently reducing optical background …

Serum protein electrophoresis (SPE) separates serum proteins into bands whose shape and
amplitude can alert clinicians to a range of disorders. This is followed by more specific …

Screening molecular libraries for ligands capable of binding proteins is widely used for hit
identification in the early drug discovery process. Oligonucleotide libraries provide a very …

One of the major difficulties that arises when selecting aptamers containing a G-quadruplex
is the correct amplification of the ssDNA sequence. Can aptamers containing a G …

The equilibrium dissociation constant (Kd) of biomolec-ular complexes is a fundamental
physicochemical parameter frequently determined in various fields of scientific research. A …

A wide range of medical conditions can be diagnosed through sequence‐specific analysis
of nucleic acids. However, a major challenge remains in detecting a specific target in …