Abstract: A method for the structure-based identification and selection of inhibitors of processivity factor binding to protein is disclosed herein. Characterization of the protein/processivity factor interface is given. Methods for the structure-based inhibition of processivity factor binding to protein are also given. One embodiment includes a class of peptidomimetics that mimic helical portions of proteins. In addition, methods of treatment of various diseases are given, using the inhibitors of the invention.

Abstract: A method for the structure-based identification and selection of inhibitors of processivity factor binding to protein is disclosed herein. Characterization of the protein/processivity factor interface is given. Methods for the structure-based inhibition of processivity factor binding to protein are also given. One embodiment includes a class of peptidomimetics that mimic helical portions of proteins. In addition, methods of treatment of various diseases are given, using the inhibitors of the invention.

Abstract: A method for the structure-based identification and selection of inhibitors of processivity factor binding to protein is disclosed herein. Characterization of the protein/processivity factor interface is given. Methods for the structure-based inhibition of processivity factor binding to protein are also given. One embodiment includes a class of peptidomimetics that mimic helical portions of proteins. In addition, methods of treatment of various diseases are given, using the inhibitors of the invention.

Abstract: This invention relates to HDAg peptides, including mutants, derivatives fragments and fusion molecules, including fusion proteins, coiled-coil oligomers, nucleic acid molecules, vectors comprising HDAg nucleic acid molecules, cells comprising said molecules, methods of multivalent expression and association of binding moieties of HDAg fusion molecules, and methods of use involving the molecules. The molecules are particularly useful as a framework for multivalent display via formation of C-terminal and/or N-terminal fusion proteins or via chemical coupling to chemically reactive sidechains, e.g. cysteine residues.

Abstract: The present invention is broadly directed to methods of screening viral-binding compounds. In particular, the present invention provides cell-free assays to rapidly screen libraries of compounds for viral-capsid binding activity. Such compounds are useful for anti-viral treatments.