Mammalian display screening of diverse cystine-dense peptides for difficult to drug targets

Nat Commun. 2017 Dec 21;8(1):2244. doi: 10.1038/s41467-017-02098-8.

Abstract

Protein:protein interactions are among the most difficult to treat molecular mechanisms of disease pathology. Cystine-dense peptides have the potential to disrupt such interactions, and are used in drug-like roles by every clade of life, but their study has been hampered by a reputation for being difficult to produce, owing to their complex disulfide connectivity. Here we describe a platform for identifying target-binding cystine-dense peptides using mammalian surface display, capable of interrogating high quality and diverse scaffold libraries with verifiable folding and stability. We demonstrate the platform's capabilities by identifying a cystine-dense peptide capable of inhibiting the YAP:TEAD interaction at the heart of the oncogenic Hippo pathway, and possessing the potency and stability necessary for consideration as a drug development candidate. This platform provides the opportunity to screen cystine-dense peptides with drug-like qualities against targets that are implicated for the treatment of diseases, but are poorly suited for conventional approaches.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cystine / analysis*
  • Drug Discovery
  • Escherichia coli Proteins / chemistry
  • Glycosylation
  • Humans
  • Peptide Library
  • Peptides / chemistry*
  • Peptides / metabolism
  • Peptides / pharmacology*
  • Protein Binding
  • Protein Folding
  • Protein Interaction Maps / drug effects*
  • Reproducibility of Results
  • Saccharomyces cerevisiae Proteins / chemistry

Substances

  • Escherichia coli Proteins
  • Peptide Library
  • Peptides
  • Saccharomyces cerevisiae Proteins
  • Cystine