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Affinity-Guided Design of Caveolin-1 Ligands for Deoligomerization.

  • Author(s): Gilliam, Amanda JH
  • Smith, Joshua N
  • Flather, Dylan
  • Johnston, Kevin M
  • Gansmiller, Andrew M
  • Fishman, Dmitry A
  • Edgar, Joshua M
  • Balk, Mark
  • Majumdar, Sudipta
  • Weiss, Gregory A
  • et al.

Published Web Location

http://media.wix.com/ugd/9ecda9_4f3a90d4c723468d9f667019742cda83.pdf
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Abstract

Caveolin-1 is a target for academic and pharmaceutical research due to its many cellular roles and associated diseases. We report peptide WL47 (1), a small, high-affinity, selective disrupter of caveolin-1 oligomers. Developed and optimized through screening and analysis of synthetic peptide libraries, ligand 1 has 7500-fold improved affinity compared to its T20 parent ligand and an 80% decrease in sequence length. Ligand 1 will permit targeted study of caveolin-1 function.

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