Asim K. Bera

Mar 18, 2024 | nature.com | Danny D. Sahtoe |Ewa Andrzejewska |Hannah Han |Matthias Schneider |Georg Meisl |Hannah Nguyen | +2 more

AbstractSegments of proteins with high β-strand propensity can self-associate to form amyloid fibrils implicated in many diseases. We describe a general approach to bind such segments in β-strand and β-hairpin conformations using de novo designed scaffolds that contain deep peptide-binding clefts. The designs bind their cognate peptides in vitro with nanomolar affinities.

Sep 13, 2023 | nature.com | Andrés Fernández |John Kraft |Viet Le |Jonard Corpuz Valdoz |Marcos Miranda |Yakov Kipnis | +7 more

AbstractThe RGD (Arg-Gly-Asp)-binding integrins αvβ6 and αvβ8 are clinically validated cancer and fibrosis targets of considerable therapeutic importance. Compounds that can discriminate between homologous αvβ6 and αvβ8 and other RGD integrins, stabilize specific conformational states, and have high thermal stability could have considerable therapeutic utility. Existing small molecule and antibody inhibitors do not have all these properties, and hence new approaches are needed.

Sep 4, 2023 | nature.com | Neville P. Bethel |Andrew J. Borst |Fabio Parmeggiani |Asim K. Bera |Marcos Miranda |Ryan Kibler | +1 more

AbstractMolecular systems with coincident cyclic and superhelical symmetry axes have considerable advantages for materials design as they can be readily lengthened or shortened by changing the length of the constituent monomers. Among proteins, alpha-helical coiled coils have such symmetric, extendable architectures, but are limited by the relatively fixed geometry and flexibility of the helical protomers.