1. Academic Validation
  2. Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation

Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation

  • J Am Chem Soc. 2007 Nov 28;129(47):14560-1. doi: 10.1021/ja076250y.
Andrew L MacKinnon 1 Jennifer L Garrison Ramanujan S Hegde Jack Taunton
Affiliations

Affiliation

  • 1 Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94158, USA.
Abstract

Photoaffinity labeling is a powerful tool to identify protein targets of biologically active small molecules, yet is often limited by the size, chemical properties, and availability of photoreactive groups. We report an improved synthesis of photo-leucine, a diazirine-based photoreactive analogue of leucine, and demonstrate its incorporation into a cyclodepsipeptide inhibitor of cotranslational translocation. Photoaffinity labeling in a crude membrane fraction, followed by "click chemistry" with a rhodamine-azide reporter, enabled the identification of Sec61alpha, the structural core of the Sec61 translocation channel, as the inhibitor's target.

Figures
Products
  • Cat. No.
    Product Name
    Description
    Target
    Research Area
  • HY-P10477
    Sec61 Modulator