Peptidomimetic inhibitors of p21ras farnesyltransferase

Hydrophobic functionalization leads to disruption of p21ras membrane association in whole cells

Yimin Qian, Michelle A. Blaskovich, Churl Min Seong, Andreas Vogt, Andrew Hamilton, Said M. Sebti

Research output: Contribution to journalArticle

Abstract

In this paper we describe the synthesis of several hydrophobic inhibitors of p21ras farnesyltransferase. These peptidomimetic structures, containing cysteine and methionine residues separated by an aromatic spacer, are functionalized as their methyl esters and N,S-bis-benzyloxycarbonyl (Cbz) derivatives and are shown to penetrate NIH 3T3 cells to disrupt p21 ras plasma membrane association.

Original languageEnglish (US)
Pages (from-to)2579-2584
Number of pages6
JournalBioorganic and Medicinal Chemistry Letters
Volume4
Issue number21
DOIs
StatePublished - Nov 10 1994

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Proto-Oncogene Proteins p21(ras)
Farnesyltranstransferase
Peptidomimetics
NIH 3T3 Cells
Cell membranes
Methionine
Cysteine
Esters
Cell Membrane
Association reactions
Derivatives
Membranes

ASJC Scopus subject areas

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

Cite this

Peptidomimetic inhibitors of p21ras farnesyltransferase : Hydrophobic functionalization leads to disruption of p21ras membrane association in whole cells. / Qian, Yimin; Blaskovich, Michelle A.; Seong, Churl Min; Vogt, Andreas; Hamilton, Andrew; Sebti, Said M.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 4, No. 21, 10.11.1994, p. 2579-2584.

Research output: Contribution to journalArticle

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