Fenretinide binding to the lysosomal protein saposin D alters ceramide solubilization and hydrolysis

Brandon T. Milliken, Lindy Melegari, Gideon L. Smith, Kris Grohn, Aaron J. Wolfe, Kelsey Moody, Fadi Bou-Abdallah, Robert P. Doyle

Research output: Contribution to journalArticlepeer-review

Abstract

Fenretinide is a synthetic retinoid pharmaceutical linked to ceramide build-up in vivo. Saposin D is an intralysosomal protein necessary for ceramide binding/degradation. We show, via electronic absorption spectroscopy, fluorescence spectroscopy, and ceramide hydrolysis assays, that fenretinide is bound by saposin D {Ka = (1.45 ± 0.49) × 105 M-1}, and affects ceramide solubilization/degradation.

Original languageEnglish (US)
Pages (from-to)1048-1052
Number of pages5
JournalRSC Medicinal Chemistry
Volume11
Issue number9
DOIs
StatePublished - Sep 2020

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science
  • Pharmacology

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