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Discovery Studio 3.5: The Latest Version of the Leading Visualization Software for Protein and Small



Discngine provides scientific computing consulting services and solutions for pharmaceutical research informatics. We are specialized in the integration of scientific software like BIOVIA Pipeline Pilot, Chemaxon, CambridgeSoft (Perkin Elmer) and industry standards like Oracle database or Tibco Spotfire. With our three key partners: BIOVIA, Tibco and Oracle we build integrated solution to address current and future challenges of the pharmaceutical discovery. In addition to the consulting services we provide, we have developed two ranges of products: - Oracle based modules designed for Plated Based Assay data acquisition, Sample Management & Decision Making. - BIOVIA Pipeline Pilot collections for enhanced Chemistry features, Graphs manipulation and the Tibco Spotfire connector


Human epidermal growth factor receptor (EGFR) is an important drug target that plays a fundamental role in signal transduction pathways in oncology. We report herein the discovery of a novel class of phenylpiperazine derivatives with improved potency toward EGFR. The biological activity of compound 3p as inhibitor of EGFR was further investigated both in vitro and in vivo. Notably, compound 3p exhibited an IC50 in the nanomolar range in A549 cell cultures and induced a cessation of tumor growth with no toxicity, as determined by loss of body weight and death of treated mice. Compoutational docking studies also showed that compound 3p has interaction with EGFR key residues in the active site.




discovery studio 3.5




Protein kinases regulate many critical cellular processes through protein phosphorylation, such as proliferation, differentiation and DNA damage/repair1 and therefore have been proved to be important drug discovery targets2,3,4,5. Among these kinases, the family of human epidermal growth factor receptor (EGFR), is an important drug target that play a fundamental role in signal transduction pathways in oncology. Deregulation of the EGFR family pathway by overexpression or constitutive activation induces numerous cancers2. All proteins in the EGFR family are transmembrane proteins, containing an extracellular ligand binding domain, a transmembrane domain, an intracellular receptor tyrosine kinase domain and a C-terminal signaling tail domain6. The members of the EGFR family share high structural homology in their tyrosine kinase domain but are distinct in their extracellular and C-terminal domains7. The binding of growth factors to the extracellular domain induces receptor homo- or heterodimerization and activates the kinase domain, which would lead to the autophosphorylation of the intracellular tyrosine residues at the C-terminal and the subsequent induction of downstream signals8,9. We therefore attempted to design and synthesize a series of novel EGFR tyrosine kinase inhibitors which could be beneficial to patients suffering from various cancers. 2ff7e9595c


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