Synthesis and screening of a CaaL peptide library versus FTase reveals a surprising number of substrates

Amanda J. Krzysiak, Animesh V. Aditya, James L. Hougland, Carol A. Fierke, Richard A. Gibbs

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

Proteins bearing a CaaL sequence are typically geranylgeranylated to enable their proper localization and function. We found that many of the dansyl-GCaaL peptides representing mammalian CaaL proteins can be farnesylated by FTase. This result may have important implications for prenylated protein biology.

Original languageEnglish (US)
Pages (from-to)767-770
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume20
Issue number2
DOIs
StatePublished - Jan 15 2010

Keywords

  • Enzymes
  • Farnesylation
  • Geranylgeranylation
  • Peptide synthesis
  • Post-translational modification

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Synthesis and screening of a CaaL peptide library versus FTase reveals a surprising number of substrates'. Together they form a unique fingerprint.

  • Cite this