Aarhus University Seal / Aarhus Universitets segl

Vitamin B12 Phosphate Conjugation and Its Effect on Binding to the Human B12 -Binding Proteins Intrinsic Factor and Haptocorrin

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

DOI

  • Keith Ó Proinsias, Institute of Organic Chemistry PAS, Kasprzaka 44/52, 01-224, Warsaw, Poland.
  • ,
  • Michał Ociepa, Institute of Organic Chemistry PAS, Kasprzaka 44/52, 01-224, Warsaw, Poland.
  • ,
  • Katarzyna Pluta, Institute of Organic Chemistry PAS, Kasprzaka 44/52, 01-224, Warsaw, Poland.
  • ,
  • Mikołaj Chromiński, Institute of Organic Chemistry PAS, Kasprzaka 44/52, 01-224, Warsaw, Poland.
  • ,
  • Ebba Nexo
  • Dorota Gryko, Institute of Organic Chemistry PAS, Kasprzaka 44/52, 01-224, Warsaw, Poland. dorot.gryko@icho.edu.pl.
The binding of vitamin B12 derivatives to human B12 transporter proteins is strongly influenced by the type and site of modification of the cobalamin original structure. We have prepared the first cobalamin derivative modified at the phosphate moiety. The reaction conditions were fully optimized and its limitations examined. The resulting derivatives, particularly those bearing terminal alkyne and azide groups, were isolated and used in copper-catalyzed alkyne-azide cycloaddition reactions (CuAAC). Their sensitivity towards light revealed their potential as photocleavable molecules. The binding abilities of selected derivatives were examined and compared with cyanocobalamin. The interaction of the alkylated derivatives with haptocorrin was less affected than the interaction with intrinsic factor. Furthermore, the configuration of the phosphate moiety was irrelevant to the binding process.
OriginalsprogEngelsk
TidsskriftChemistry: A European Journal
Vol/bind22
Nummer24
Sider (fra-til)8282-9
Antal sider8
ISSN0947-6539
DOI
StatusUdgivet - 6 jun. 2016

    Forskningsområder

  • Click Chemistry, Glycoproteins, Phosphates, Substituent effects, Vitamins

Se relationer på Aarhus Universitet Citationsformater

ID: 107916517