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The β-d-Glucose Scaffold as a β-Turn Mimetic
Accounts of Chemical Research (2009)
  • Ralph F. Hirschmann, University of Pennsylvania
  • K.C. Nikolaou, The Scripps Research Institute
  • Angie R. Angeles, University of Pennsylvania
  • Jason Chen, The Scripps Research Institute
  • Amos B. Smith, III, University of Pennsylvania
Activity and selectivity are typically the first considerations when designing a drug. However, absorption, distribution, metabolism, excretion, and toxicity (ADMET) are equally important considerations. Peptides can provide a combination of potent binding and exquisite selectivity, as evidenced by their pervasive use as enzymes, hormones, and signaling agents within living systems. In particular, peptidic turn motifs are key elements of molecular recognition. They may be found at the exposed surfaces of globular proteins, where they are available for binding interactions with other peptides and small molecules.
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Publisher Statement
Reprinted (adapted) with permission from Acc. Chem. Res., 2009, 42 (10), pp 1511–1520. Copyright 2009 American Chemical Society.
Citation Information
Ralph F. Hirschmann, K.C. Nikolaou, Angie R. Angeles, Jason Chen, et al.. "The β-d-Glucose Scaffold as a β-Turn Mimetic" Accounts of Chemical Research Vol. 42 Iss. 10 (2009) p. 1511 - 1520
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