Valorisation-recherche, Limited Partnership

Universitéde Montreal

Université Paul Sabatier (toulouse Iii)

Micronics, Inc.

Valorisation Hsj, Limited Partnership

Jurgen Sygusch

Bernhard Hans Weigl

Caroline Alfieri

Nico Blom

Mathieu Coinçon

Laurent Azema

Jing Hu

Chantal Dax

Jerome Tanner

Casimir Blonski

The present invention relates to a peptide comprising (A) (i) a first domain comprising an amino acid sequence having at least 60% sequence similarity with the sequence PDDRTLQ (SEQ ID NO:1); and (ii) a second domain covalently linked to the first domain and comprising an amino acid sequence having at least 60% sequence similarity with the sequence QNPVYLIPETVPYIKWDN (SEQ ID NO:2) or (B) (i) a first domain comprising an amino acid sequence having at least 60% sequence similarity with the sequence GSAKPGNGSYF (SEQ ID NO: 41); and (ii) a second domain covalently linked to the first domain, said second domain comprising an amino acid sequence having at least 60% sequence similarity with the sequence SVKTEMLGNEID (SEQ ID NO: 42), wherein the peptide binds to monoclonal antibody clone 72A1. This peptide may be useful for inducing the production of neutralizing antibodies against a gp350-expressing herpesvirus, such as Epstein-Barr virus (EBV), for example for immunizing or vaccinating an animal against a gp350-expressing herpesvirus, as well as for detecting the presence or absence neutralizing anti-gp350-expressing herpesvirus antibodies in a sample.

Antigenic epitopes from EBV gp350/220 and uses thereof

The invention relates to novel aldolase-inhibiting compounds that can be advantageously used as medicaments (in therapeutic doses), especially for treating certain cancers, due to the inhibition efficacy thereof. An inventive compound corresponds to general formula (I) wherein the aldehyde group (&#x2014;CHO) and the phenol group (&#x2014;OH) are linked to two carbon atoms adjacent to the same aromatic chain, i.e., the first aromatic chain, and R is a phosphate group or a phosphate group mimetic linked to a carbon atom of the second aromatic chain.

Aldolase-inhibiting aromatic compounds

A device for promoting protein crystal growth (PCG) using microfluidic channels. A protein sample and a solvent solution are combined within a microfluidic channel having laminar flow characteristics which forms diffusion zones, providing for a well defined crystallization. Protein crystals can then be harvested from the device. The device is particularly suited for microgravity conditions.

Protein crystallization in microfluidic structures

A `docking` method based on finite grid forcefield sampling makes use of fast evaluation of interaction energies between molecules, such as macromolecules and ligands. The forcefield used to calculate interaction energies utilizes a potential energy function composed of a 1/r dependent electrostatic term and a (6-12) Lennard-Jones term for Van der Waals interactions. Successful prediction of ligand position and determination of ligand-protein interaction enthalpy is done by mapping potential energy field components of one of the molecules onto a energy field component grids, and mapping interaction field components of another of the two molecules onto interaction component grids. By calculating a correlation between each potential energy field component grid and each interaction field grid, a plurality of grids of molecule binding energy values is obtained which represent a binding energy of the two molecules in the given relative rotation between the molecules for each relative translational positions in space between the molecules. At least one maximum of the binding energy values is determined and the relative translational positions for the maximum binding energy values are recorded. By rotating at least one of the molecules according to each relative rotation in a range of rotation, and by repeating the mapping for the rotated molecule and subsequently repeating the calculating and determining for each of the relative rotations, it is possible to select an energetically favorable one of the relative rotations and the relative translational positions to generate a position value for an energetically favorable binding site between the two molecules.

Energetically favorable binding site determination between two molecules

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Montreal, Canada

Jurgen Sygusch