Sylvie Derclaye

TL;DR: It is demonstrated, both on model surfaces and on living cells, that the receptor binding domain (RBD) serves as the binding interface within the S-glycoprotein with the ACE2 receptor and the kinetic and thermodynamic properties of this binding pocket are extracted.

TL;DR: The results are discussed in terms of a possible organization of the antiparallel beta-sheets in Abeta oligomers, which may be related to reported effects of these highly toxic species in the amyloid pathogenesis associated with AD.

TL;DR: Although this work focuses mainly on the probiotic bacterium Lactobacillus plantarum, it is shown that the procedures are applicable to pathogens, such as the bacterium Staphylococcus epidermidis and the yeast Candida albicans.

TL;DR: In this article, the surface of polystyrene (PSox) was investigated using X-ray photoelectron spectroscopy (XPS), streaming potential measurements and a dynamic study of the wetting properties at different pH (Wilhelmy plate method).

TL;DR: This structural study suggests that conversion of oligomers into fibrils results from a transition from antiparallel to parallel β-sheet, which could be a generic mechanism determining the kinetics of protein misfolding in Alzheimer's disease.