Assessing helical protein interfaces for inhibitor design

Brooke N. Bullock, Andrea L. Jochim, Paramjit Arora

Research output: Contribution to journalArticle

Abstract

Structure-based design of synthetic inhibitors of protein-protein interactions (PPIs) requires adept molecular design and synthesis strategies as well as knowledge of targetable complexes. To address the significant gap between the elegant design of helix mimetics and their sporadic use in biology, we analyzed the full set of helical protein interfaces in the Protein Data Bank to obtain a snapshot of how helices that are critical for complex formation interact with the partner proteins. The results of this study are expected to guide the systematic design of synthetic inhibitors of PPIs. We have experimentally evaluated new classes of protein complexes that emerged from this data set, highlighting the significance of the results described herein.

Original languageEnglish (US)
Pages (from-to)14220-14223
Number of pages4
JournalJournal of the American Chemical Society
Volume133
Issue number36
DOIs
StatePublished - Sep 14 2011

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ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Assessing helical protein interfaces for inhibitor design. / Bullock, Brooke N.; Jochim, Andrea L.; Arora, Paramjit.

In: Journal of the American Chemical Society, Vol. 133, No. 36, 14.09.2011, p. 14220-14223.

Research output: Contribution to journalArticle

Bullock, Brooke N. ; Jochim, Andrea L. ; Arora, Paramjit. / Assessing helical protein interfaces for inhibitor design. In: Journal of the American Chemical Society. 2011 ; Vol. 133, No. 36. pp. 14220-14223.
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