Heat release at the wetting front during capillary filling of cellulosic micro-substrates.

Spontaneous imbibition in cellulosic materials is an expanding field of research due to the direct applicability in paper-based microfluidics. Here, we show experimentally, using simultaneous thermal and optical imaging that the temperature at the wetting front during capillary filling of paper is temporarily increased, even if the imbibed fluid and the cellulosic substrate are initially at isothermal conditions. Several liquids and two types of filter paper, characterised by scanning electron microscopy (SEM) and X-ray diffraction (XRD) analysis, were investigated demonstrating a significant temperature rise at the wetting front that cannot be neglected form the process.

A bispecific HER2-targeting FynomAb with superior antitumor activity and novel mode of action.

Upregulation of HER2 is a hallmark of 20% to 30% of invasive breast cancers, rendering this receptor an attractive target for cancer therapy. Although HER2-targeting agents have provided substantial clinical benefit as cancer therapeutics, there is a need for the development of new agents aiming at circumventing anti-HER2 resistance. On the basis of the approved antibody pertuzumab, we have created a panel of bispecific FynomAbs, which target two epitopes on HER2.

Mapping the conformational space accessible to BACE2 using surface mutants and cocrystals with Fab fragments, Fynomers and Xaperones.

The aspartic protease BACE2 is responsible for the shedding of the transmembrane protein Tmem27 from the surface of pancreatic β-cells, which leads to inactivation of the β-cell proliferating activity of Tmem27. This role of BACE2 in the control of β-cell maintenance suggests BACE2 as a drug target for diabetes. Inhibition of BACE2 has recently been shown to lead to improved control of glucose homeostasis and to increased insulin levels in insulin-resistant mice.

Generation, characterization and structural data of chymase binding proteins based on the human Fyn kinase SH3 domain.

The serine protease chymase (EC = 3.4.21.