Publication25 July 2019Gradient-free determination of isoelectric points of proteins on chip
Lapinska et al. using a microfluidic system built in house design a new technique to determine a protein's isoelectric point (pI) based on microfluidic free-flow electrophoresis (μFFE). The approach exploits temporal rather than spatial pH gradients. To demonstrate the effectiveness of this method the pI of 7 different proteins of known pI were tested; β-lactoglobulin, ribonuclease A, ovalbumin, human transferrin, ubiquitin and myoglobin. The paper shows that this method is successful in determining the pI using this new technique without the requirement of generating and maintaining pH gradients which is often challenging for other techniques. The technique requires low voltages and low sample consumption. The paper also shows that using this technique it is possible to estimate the pI values for a wide range of proteins measuring at only two pH values, suggesting that this technique is rapid and accurate on small volume samples.
Publication25 July 2019Microfluidic diffusional sizing (MDS) in the literature
Document referencing all the publications where microfluidic diffusional sizing (MDS) has been used.
Publication24 July 2019Putative interaction site for membrane phospholipids controls activation of TRPA1 channel at physiological membrane potentials.
Macikova et al use Microfluidic Diffusional Sizing (MDS) along with other techniques to understand the role phosphatidylinositol-4,5-bisphosphate (PIP2) has in the regulation of transient receptor potential ankyrin 1 (TRPA1) channel. The Fluidity One was used to create binding curves of the interactions between two specific peptides (L992-N1008 and T1003-P1034) and model lipid membranes in the presence of PIP2.
Publication04 June 2019Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates
In this paper MDS was used to identify two molecular chaperones which suppress secondary nucleation processes and inhibit the elongation of Aβ fibrils seen in Alzheimer's disease.
Publication06 March 2019α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation
This paper probes the interactions of α-synuclein with lipid particles using the Fluidity One and various other methods, to investigate the link between these interactions and α-synuclein aggregation.