Science Direct July 6, 2022
A team of researchers in the US (City College of New York, The State University of New Jersey, Clarkson University) designed a pair of VX-binding proteins using a supercharged scaffold that coupled a large-scale phase change from unstructured to folded upon ligand binding, enabling fully internal binding sites that present the maximum surface area possible for high affinity and specificity in target recognition. Binding site residues were chosen using a new distributed evolutionary algorithm implementation in protCAD. Both designs detected VX at parts per billion concentrations with high specificity. Computational design of fully buried molecular recognition sites, in combination with supercharged phase-changing chassis proteins, enabled the ready development of a new generation of small-molecule biosensors…read more. Open Access TECHNICAL ARTICLEÂ
The VX nerve agent, its simulants, and breakdown products. Credit: SCIENCE ADVANCES, 6 Jul 2022, Vol 8, Issue 27Â