12-Substituted-13,14-dihydroretinols designed for affinity labeling of retinol binding- and processing proteins

Revital Yefidoff, Amnon Albeck

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


All-trans- and 11-cis-retinol derivatives substituted with various electron-withdrawing groups at C 12 were designed to be affinity labels for retinol binding and processing proteins. Unlike other non-selective highly reactive affinity labels, these compounds carry a Michael acceptor type substitution at C 12 of the polyene chain. Therefore, they are expected to be highly selective towards such proteins that have a nucleophilic residue near the C 11 position of their retinol ligand. The synthetic route for these compounds is based on the Emmons-Horner reaction of a C15 aldehyde with an appropriate phosphonate bearing the desired electron-withdrawing group to be incorporated at the C 12 position of the retinol skeleton. Graphical abstract

Original languageEnglish
Pages (from-to)8093-8102
Number of pages10
Issue number37
StatePublished - 6 Sep 2004

Bibliographical note

Funding Information:
This research was supported by a United States-Israel Binational Science Foundation grant no. 2000390.


  • Affinity labeling
  • Michael acceptors
  • Retinol analogs
  • Retinol binding proteins
  • trans Retinyl ester isomerohydrolase


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