A nanobody-based microfluidic chip for fast and automated purification of protein complexes.

Many proteins, especially eukaryotic proteins, membrane proteins and protein complexes, are challenging to study because they are difficult to purify in their native state without disrupting the interactions with their partners. Hence, our lab developed a novel purification technique employing Nanobodies® (Nbs). This technique, called nanobody exchange chromatography (NANEX), utilises an immobilised low-affinity Nb to capture the target protein, which is subsequently eluted - along with its interaction partners - by introducing a high-affinity Nb.

Solvent-free confinement of ordered microparticle monolayers: effect of host substrate and pattern symmetry.

The self-organisation of individual suspended colloids into ordered structures that can be mediated by confinement has garnered interest recently. Despite the push for solvent reduction for sustainability reasons, the comprehension and development of solvent-free assembly methods remain largely unaddressed. In this study, we explore the effect of confinement without rigid geometrical constraints, , wall-less confinement on the assembly of monodisperse PMMA powder microspheres (diameters of 3 μm and 10 μm) on fluorocarbon-patterned heterogeneous substrates using a solvent-free rubbing assembly approach.

Motion tracking with automated pose estimator can enhance ankle-foot-orthoses alignment.

Background: Ankle-foot orthoses are commonly prescribed to address motor impairments in individuals with neurological disorders. Proper alignment of Ankle-foot orthoses, commonly assessed by the ground reaction force in relation to the knee joint center and the shank-to-vertical angle, is crucial for their effectiveness but is time-consuming. This study validates automated pose estimator DeepLabCut on measuring these metrics using 2D videos with force vector overlay in individuals with neurological disorders wearing ankle-foot orthoses.

Structure-Function Relationship of a Novel MTX-like Peptide (MTX1) Isolated and Characterized from the Venom of the Scorpion .

Maurotoxin (MTX) is a 34-residue peptide from venom. It is reticulated by four disulfide bridges with a unique arrangement compared to other scorpion toxins that target potassium (K) channels. Structure-activity relationship studies have not been well performed for this toxin family.