VeraChem LLC founders Drs. Michael Gilson, Michael Potter, and Hillary Gilson, using UMBI licensed intellectual property, are creating scientific software that provides expert users with tools for computer-aided drug discovery and molecular design. VeraChem’s recent first sale, a pre-release version of Vconf, is followed by the projected launch on September 8 of Vcharge, a new software product for computing molecular properties important in drug design. The official launch of Vconf is expected to follow later in 2004.
“Vcharge combines speed and accuracy in a unique software package that will be available for the Linux and Windows operating systems,” says Dr. Gilson, Chief Scientific Officer for VeraChem LLC and Professor at UMBI’s Center for Advanced Research in Biotechnology. “This product is just the first in a series that will bring advanced computational methods in an affordable and user-friendly format to experts in the pharmaceutical and biotechnology industries.”
“Vcharge is a tool for computer-aided drug design,” says Dr. Gilson. “It allows the designer to compute the atomic charges of a candidate drug molecule as a step in determining whether it will effectively bind a targeted protein. Most drugs work by binding tightly to a targeted protein molecule. For example, HIV protease inhibitors help patients by binding and blocking the function of a protein that the AIDS virus needs to survive and reproduce. Each atom of a protein carries a small electrical charge and, since opposite charges attract while like charges repel, it is important that the atoms of a drug molecule have charges which complement the targeted protein.”
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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