Prion versus doppel protein misfolding: new insights from replica-exchange molecular dynamics simulations.

The doppel (Dpl) and prion (PrP) proteins share a very similar fold (three helices and two short β-strands), while they differ significantly in sequence (only 25% homologous) and in disease-related β-rich conformations that occur for PrP only. In a previous study [Baillod, P., et al.

Enhanced sampling molecular dynamics identifies PrP(Sc) structures harboring a C-terminal β-core.

We perform a replica exchange molecular dynamics simulation corresponding to a 2.8 μs total time for the extensive enhanced sampling of the conformational space of the C-terminal part (residues 124-226) of the mouse prion protein (PrP); 1.3% of the conformations sampled display a high level of β-structure (≥19 residues), allowing the assessment of β-propensities along the sequence and highlighting the most structurally labile hot spots.

Biochemical properties of the fibrinogen component of a fibrin glue before and after severe dry heat treatment.

Functional biochemical properties of 5 batches of the fibrinogen component of a fibrin glue produced by the ZLB Central Laboratory, Bern, each consisting of 4 different in-process samples (taken after the first and second precipitation step, lyophilization, and dry-heat treatment) were studied in vitro. We focused our attention on the effect of the anti-viral treatment of the lyophilized product by dry heat for 1 h at 100 degrees C. A slight reduction in maximal turbidity of all heat-treated samples was observed during the clotting assay compared to nontreated samples.

New variant of type II von Willebrand's disease with structural abnormality of plasma von Willebrand factor in a patient with very mild bleeding history.

A new variant of von Willebrand's disease has been discovered in 2 members of a Macedonian family of 6. The proband, an 8-year-old boy, showed a prolonged bleeding episode on 1 occasion. Ristocetin-induced platelet aggregation and bleeding time were normal.

Quantitative and qualitative analysis of platelet GPIb and von Willebrand factor in liver cirrhosis.

Numerous abnormalities of plasmatic coagulation and platelet function may contribute to the bleeding in liver cirrhosis with a defective platelet-von Willebrand factor interaction being a potential mechanism. To analyze GPIb and von Willebrand factor in cirrhosis, we quantified the number of GPIb molecules on the platelet surface by flow cytometry, assessed the total (and indirectly the internal) pool of GPIb by ELISA and measured the circulating amount of glycocalicin in plasma as a measure of proteolytic activity and platelet turnover. Von Willebrand factor was characterized by ELISA, by its ristocetin-cofactor activity and by multimer analysis.