Limiting Assumptions in the Design of Peptidomimetics

Garland R. Marshall, Flavio Ballante

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

(Table presented.). Limiting the flexibility of organic compounds to enhance their affinity and selectivity for targeting a macromolecule involved in molecular recognition has become a well-developed paradigm in medicinal chemistry. While the role of reverse-turn motifs as peptidomimetics has received the most attention, β-sheets and helices are also important motifs for protein/protein interactions. The more complicated problem of mimicking the interacting surface of noncontiguous epitopes will not be considered in this review. This limited overview focuses on efforts to use amino acid synthons as secondary-structure mimetics as well as providing examples of peptidomimetic design focused on nonpeptide synthetic chemistry in contrast. In particular, the rationale of optimal design criteria for mimicry and the many naïve violations of those criteria made in its pursuit are emphasized. Drug Dev Res 78 : 245–267, 2017.

Original languageEnglish
Pages (from-to)245-267
Number of pages23
JournalDrug Development Research
Volume78
Issue number6
DOIs
StatePublished - Sep 2017

Keywords

  • beta-sheet mimetics
  • helix mimetics reverse-turn mimetics
  • semi-rigid analogs

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