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Palaiseau, France
Palaiseau, France
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News Article | November 16, 2016
Site: www.prweb.com

The new TRITON Portable sewer camera is a logical continuation of the Triton product line of heavy-duty drain and sewer inspection systems. This unit is made in Canada and combines portability and compact size with the traditional rugged design and extreme durability. The stainless steel camera head, protected with an anti-scratch sapphire lens is 1.23’’ in diameter. The metal coil right behind the camera adds flexibility and makes it easier for the camera to navigate bends and corners. The camera head features an integrated 512Hz sonde transmitter or beacon compatible with any locator of the same frequency. The advanced ¼ CCD sensor ensures a high quality image. The camera DVR comes in machined aluminum housing for increased durability. It has a large 7.4’’ color display protected with an acrylic cover. Unlike most comparable products the new TRITON is equipped with a wifi module in order to establish a connection between the unit and a smartphone, tablet or any other mobile device. This way the user can visualize and record the inspection remotely. The still images and video recordings can also be stored on a USB memory stick. A separate USB recording feature is available as an option. In addition, the camera controller possesses an on-screen footage counter and an on-screen text generator to take notes directly during the inspection. The 125’ (38 meters) long push rod is placed on a solid reel made of powder coated steel tube frame. The push cable is Kevlar braided for increased protection and longevity. The total weight of the unit is only 29 lbs. (just over 13 kg). The new TRITON Portable sewer camera is a highly reliable inspection tool. It is made exclusively of durable, solid components and does not contain any plastic, breakable parts. It is designed particularly for pipes between 1.5’’ and 6’’ in diameter depending on the pipe configuration and the presence of bends and corners. Fiberscope.net is the industrial division of MEDIT and one of the leading suppliers of equipment for remote visual inspection. Operating from two facilities located in Boston, USA and Winnipeg, Canada, MEDIT serves an international market and offers reliable borescopes, fiberscopes and inspection cameras. TRITON is a premium line of cameras for pipe and duct inspection.


Doppelt-Azeroual O.,University Paris Diderot | Doppelt-Azeroual O.,MEDIT SA | Delfaud F.,MEDIT SA | Moriaud F.,MEDIT SA | De Brevern A.G.,University Paris Diderot
Protein Science | Year: 2010

Ligand-protein interactions are essential for biological processes, and precise characterization of protein binding sites is crucial to understand protein functions. MED-SuMo is a powerful technology to localize similar local regions on protein surfaces. Its heuristic is based on a 3D representation of macromolecules using specific surface chemical features associating chemical characteristics with geometrical properties. MED-SMA is an automated and fast method to classify binding sites. It is based on MED-SuMo technology, which builds a similarity graph, and it uses the Markov Clustering algorithm. Purine binding sites are well studied as drug targets. Here, purine binding sites of the Protein DataBank (PDB) are classified. Proteins potentially inhibited or activated through the same mechanism are gathered. Results are analyzed according to PROSITE annotations and to carefully refined functional annotations extracted from the PDB. As expected, binding sites associated with related mechanisms are gathered, for example, the Small GTPases. Nevertheless, protein kinases from different Kinome families are also found together, for example, Aurora-A and CDK2 proteins which are inhibited by the same drugs. Representative examples of different clusters are presented. The effectiveness of the MED-SMA approach is demonstrated as it gathers binding sites of proteins with similar structure-activity relationships. Moreover, an efficient new protocol associates structures absent of cocrystallized ligands to the purine clusters enabling those structures to be associated with a specific binding mechanism. Applications of this classification by binding mode similarity include target-based drug design and prediction of cross-reactivity and therefore potential toxic side effects. © 2010 The Protein Society.


Moriaud F.,Felix Concordia SARL | Moriaud F.,MEDIT SA | Adcock S.A.,Felix Concordia SARL | Adcock S.A.,MEDIT SA | And 5 more authors.
ACS Symposium Series | Year: 2011

Through database mining of the Protein Data Bank (PDB), protein pocket similarities and 3D structural alignments of similar pockets can be performed. These 3D structural alignments can serve as guides in drug design. The commercial MED-SuMo software performs superimposition of PDB ligands based on the ligand-binding corresponding pockets' and subpockets' 3D similarities. Subpockets are occupied by fragment-like molecules or portion of ligands. The mining of such fragments' interaction with the macromolecule surface serves as both a target-based and fragment-based computational method for PDB mining. In this work, we describe two practical applications: (1) a ligand-based drug design technique for bioisosteric replacement and compound library design and (2) a computational fragment-based drug design protocol for target-based drug design scenarios : ligand design, ligand decoration and compound library design. The bioisosteric approach is based on a database of bioisosteric replacement rules which were dervived from the entire PDB and are applicable to any ligand with a known or predicted 3D bound conformation. We present two successful applications: the design of alkenyldiarylmethane ligands for HIV-RT, and the design of a small compound library for HSP90. A case study using the computational Fragment-Based Drug Design approach, was applied to the design of compounds for three types of protein target: Protein kinase, GPCR and kinesin. © 2011 American Chemical Society.


PubMed | MEDIT SA
Type: Journal Article | Journal: Briefings in bioinformatics | Year: 2011

Predicting off-targets by computational methods is gaining increasing interest in early-stage drug discovery. Here, we present a computational method based on full 3D comparisons of 3D structures. When a similar binding site is detected in the Protein Data Bank (PDB) (or any protein structure database), it is possible that the corresponding ligand also binds to that similar site. On one hand, this target hopping case is probably rare because it requires a high similarity between the binding sites. On the other hand, it could be a strong rational evidence to highlight possible off-target reactions and possibly a potential undesired side effect. This target-based drug repurposing can be extended a significant step further with the capability of searching the full surface of all proteins in the PDB, and therefore not relying on pocket detection. Using this approach, we describe how MED-SuMo reproduces the repurposing of tadalafil from PDE5A to PDE4A and a structure of PDE4A with tadalafil. Searching for local protein similarities generates more hits than for whole binding site similarities and therefore fragment repurposing is more likely to occur than for drug-sized compounds. In this work, we illustrate that by mining the PDB for proteins sharing similarities with the hinge region of protein kinases. The experimentally validated examples, biotin carboxylase and synapsin, are retrieved. Further to fragment repurposing, this approach can be applied to the detection of druggable sites from 3D structures. This is illustrated with detection of the protein kinase hinge motif in the HIV-RT non-nucleosidic allosteric site.


PubMed | MEDIT SA
Type: Journal Article | Journal: Journal of computer-aided molecular design | Year: 2012

Eg5, a mitotic kinesin exclusively involved in the formation and function of the mitotic spindle has attracted interest as an anticancer drug target. Eg5 is co-crystallized with several inhibitors bound to its allosteric binding pocket. Each of these occupies a pocket formed by loop 5/helix alpha2 (L5/alpha2). Recently designed inhibitors additionally occupy a hydrophobic pocket of this site. The goal of the present study was to explore this hydrophobic pocket with our MED-SuMo fragment-based protocol, and thus discover novel chemical structures that might bind as inhibitors. The MED-SuMo software is able to compare and superimpose similar interaction surfaces upon the whole protein data bank (PDB). In a fragment-based protocol, MED-SuMo retrieves MED-Portions that encode protein-fragment binding sites and are derived from cross-mining protein-ligand structures with libraries of small molecules. Furthermore we have excluded intra-family MED-Portions derived from Eg5 ligands that occupy the hydrophobic pocket and predicted new potential ligands by hybridization that would fill simultaneously both pockets. Some of the latter having original scaffolds and substituents in the hydrophobic pocket are identified in libraries of synthetically accessible molecules by the MED-Search software.

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