Picodiscs for facile protein-glycolipid interaction analysis.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
  • Additional Information
    • Source:
      Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370536 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-6882 (Electronic) Linking ISSN: 00032700 NLM ISO Abbreviation: Anal Chem Subsets: MEDLINE
    • Publication Information:
      Original Publication: Washington, American Chemical Society.
    • Subject Terms:
    • Abstract:
      Protein interactions with glycolipids are implicated in diverse cellular processes. However, the study of protein-glycolipid complexes remains a significant experimental challenge. Here, we describe a powerful new assay that combines electrospray ionization mass spectrometry (ESI-MS) and picodiscs, which are composed of human sphingolipid activator protein saposin A and a small number of phospholipids, to display glycolipids in a lipid environment for protein-glycolipid interaction studies in aqueous solution. Time-resolved measurements of enzyme catalyzed hydrolysis of glycolipid substrates and the detection of low, moderate, and high affinity protein-glycolipid interactions serve to demonstrate the reliability and versatility of the assay.
    • Grant Information:
      Canada Canadian Institutes of Health Research
    • Accession Number:
      0 (Glycolipids)
      0 (Saposins)
      EC 3.2.1.18 (Neu3 protein, human)
      EC 3.2.1.18 (Neuraminidase)
    • Publication Date:
      Date Created: 20150325 Date Completed: 20151130 Latest Revision: 20150421
    • Publication Date:
      20221213
    • Accession Number:
      10.1021/acs.analchem.5b00170
    • Accession Number:
      25803566