Stabilized bioactive peptides and methods of identification, synthesis, and use
AssigneeUniversity of Georgia Research Foundation, Inc.
InventorElliot Altman
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Abstract
An intracellular selection system allows screening for peptide bioactivity and stability. Randomized recombinant peptides are screened for bioactivity in a tightly regulated expression system, preferably derived from the wild-type lac operon. Bioactive peptides thus identified are inherently protease- and peptidase-resistant. Also provided are bioactive peptides stabilized by a stabilizing group at the N-terminus, the C-terminus, or both. The stabilizing group can be a small stable protein, such as the Rop protein, glutathione sulfotransferase, thioredoxin, maltose binding protein, or glutathione reductase, an α-helical moiety, or one or more proline residues.
Claims6
A polypeptide comprising a bioactive peptide, a first stabilizing group coupled to a terminus of said bioactive peptide, and a second stabilizing group coupled to the other terminus of said bioactive peptide, wherein said first stabilizing group is heterologous to the bioactive peptide and lacks the capacity to participate in the formation of an intramolecular disulfide bond within the polypeptide, wherein the second stabilizing group is heterologous to the bioactive peptide, and wherein said second stabilizing group is Xaa-Pro-Pro- or -Pro-Pro-Xaa, wherein Xaa is any amino acid.
A polypeptide comprising a bioactive peptide and a stabilizing group coupled to one or both of said bioactive peptide's termini, wherein said stabilizing group is heterologous to said bioactive peptide and consists of Xaan-Pro-Pro- or -Pro-Pro- Xaan, wherein Xaa is any amino acid and n=1 or 2.
Dependencies are inferred from the claim text.