Maastricht Economic and social Research and  training centre on Innovation and Technology

Devil in the Data
When it comes to fully understanding intra-European mobility, we still have a surprisingly long way to go…

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All headlines
  • Facebook to exclude billions from European privacy laws
  • Plastic-eating enzyme holds promise in fighting pollution
  • New oil spill clean-up 'sponge' created from waste
  • Japan's rare-earth mineral deposit can supply the world for centuries
  • Cutting-edge microscope spies on living cells inside the body
  • How to bend and stretch a diamond
  • A simple switch lets an appetite regulator linger
    Scientists have devised a simple technique for shielding biologically important molecules from degradation, which could open the door to longer-lasting drugs.

    Short chains of amino acids called peptides help to control processes ranging from food intake to communication between neurons. But many natural enzymes in the body snip peptides apart, limiting their use in medicine. Researchers from the University of Pennsylvania in Philadelphia tried a simple fix: substituting sulfur for the oxygen atom located at a peptide bond often sliced by enzymes.

    Making the atomic swap in glucagon-like peptide-1, which helps to regulate blood-sugar levels and appetite, rendered the modified peptide as much as 750 times more stable than the natural variety. Rats treated with the more durable form of the peptide had smaller blood-sugar spikes after meals than rats treated with the naturally occurring peptide.

    Nature / Journal of the American Chemical Society    November 28, 2017