Designing βpep peptides: A rational approach to the discovery of novel pharmaceutical agents and small molecules

Kevin H. Mayo, Arjan W. Griffioen

Research output: Contribution to journalReview articlepeer-review

3 Scopus citations

Abstract

Approaches to drug discovery are varied and range from high-throughput screening of small molecule databases to rational design. This review is focused on our use of structural biology and principles of protein folding to rationally design novel peptides (βpep peptides) as potential pharmaceutical drugs. βpep peptides generally fold as β-sheets that can be used as a scaffold with which to present amino acid residues in a functionally relevant fashion, thereby eliciting a desired biological activity. Presently, βpep peptides can function as antibacterials, antiangiogenics, as well as antitumor and anticoagulation agents. Our design approach also allows for relatively easy development of structure-activity relationships, identification of pharmacophore sites and reduction of peptides to smaller molecules.

Original languageEnglish (US)
Pages (from-to)337-346
Number of pages10
JournalDrugs of the Future
Volume28
Issue number4
DOIs
StatePublished - Apr 1 2003

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