We report a strategy for stabilizing peptide macrocycles by introducing side-chain-to-side-chain staples, producing peptide bicycles with higher affinity, selectivity, and resistance to degradation. We have applied this strategy to develop a small, serum-stable peptide bicycle that inhibits Grb2-SH2 60-fold more potently and 200-fold more selectively than a parent peptide.

Peptide bicycles that inhibit the Grb2 SH2 domain

245th National Meeting (2013)

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