The tedious laboratory trial-and-error method for refining protein/peptide-based medicines could be accelerated and complemented by an innovative in silico (on computer) protein design method, according to researchers at Princeton University, the University of Pennsylvania School of Medicine, and the University of California at Riverside.
Their findings, appearing in a recent issue of the Journal of the American Chemical Society, could drastically decrease the time it takes to move potential biopharmaceuticals from the drawing board to the drug store. In this study, the researchers modeled a peptide (a chain of amino acids, such as a protein or protein fragment) called Compstatin, which prevents the autoimmune-mediated damage of organs during transplantation, and various inflammatory diseases. The computer modeling and optimization process cut down on trial and error and created a version of Compstatin seven times more efficient and stable than the original.
Since the function of a peptide depends on its form, the researchers modeled the effects of substituting each of Compstatins 13 amino acid subunits with a different amino acid. The novel in silico sequence design method could then model how the altered amino acid sequence folds together in comparison to the original peptide.
Greg Lester | University of Pennsylvania
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Researchers at the University of New Hampshire have captured a difficult-to-view singular event involving "magnetic reconnection"--the process by which sparse particles and energy around Earth collide producing a quick but mighty explosion--in the Earth's magnetotail, the magnetic environment that trails behind the planet.
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Faster and secure data communication: This is the goal of a new joint project involving physicists from the University of Würzburg. The German Federal Ministry of Education and Research funds the project with 14.8 million euro.
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On Saturday, 10 November 2018, the research icebreaker Polarstern will leave its homeport of Bremerhaven, bound for Cape Town, South Africa.
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