Designing peptide receptor agonists and antagonists

Victor J. Hruby

Research output: Contribution to journalReview articlepeer-review

313 Scopus citations


The most ubiquitous mode for controlling and modulating cellular function, intercellular communication, immune response and information-transduction pathways is through peptide-protein non-covalent interactions. Hormones, neurotransmitters, antigens, cytokines and growth factors represent key classes of such peptide ligands. These ligands might either be processed fragments of larger precursor proteins or surface segments of larger proteins. Athough there are numerous exceptions, such as insulin, oxytocin and calcitonin, most ligands are not used directly as drugs, and often the most useful ligands for therapy would be analogues that act as antagonists of the native ligands. A search for systematic structure-based or ligand-based approaches to designing such ligands has been an important concern. Today, a robust strategy has been developed for the design of peptides as drugs, drug candidates and biological tools. This strategy includes structural, conformational, dynamic and topographical considerations.

Original languageEnglish (US)
Pages (from-to)847-858
Number of pages12
JournalNature Reviews Drug Discovery
Issue number11
StatePublished - Nov 2002

ASJC Scopus subject areas

  • Pharmacology
  • Drug Discovery


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