Chemical Tools to Probe Composition and Dynamics of Lipid Microdomains in Living Cells


Cells of living organisms are surrounded by a plasma membrane, which is composed of a lipid bilayer and integral membrane proteins. The structural organisation of lipids and proteins within a membrane plays a crucial role for intercellular interactions and signal transduction. In this regard, glycosphingolipids are of special interest, as they combine with cholesterol, ceramide and selected membrane proteins to form so-called lipid microdomains, which show different properties as compared to the surrounding lipid bilayer. To study this in more detail, modified glycosphingolipids are synthesised and applied to living cells. After their incorporation into the plasma membrane, they are labeled with a fluorescent dye and localized by fluorescence microscopy. This will give new insights into the distribution of glycosphingolipids, composition of lipid microdomains, and their role in biological processes such as bacterial infection.

  • Dauner, Martin - Project leader
  • Department of Chemistry
  Haddoub, Rose; Dauner, Martin; Stefanowicz, Fiona A.; Barattini, Valeria; Laurent, Nicolas; Flitsch, Sabine L. (2009): Enzymatic synthesis of peptides on a solid support Organic & Biomolecular Chemistry. 2009, 7(4), pp. 665-670. Available under: doi: 10.1039/B816847D

Enzymatic synthesis of peptides on a solid support


We have previously shown that dipeptides can be synthesised in high yields from amino acids using protease catalysis in aqueous media, if the amino component is immobilised on porous PEGA resin (a copolymer of polyethylene glycol and polyacrylamide). Here we explore the scope of this methodology for using protected and glycosylated amino acids as well as the synthesis of longer peptides on resin and show that such a method can also be applied on non-porous surfaces, in particular on gold.

Origin (projects)

Funding sources
Name Finanzierungstyp Kategorie Project no.
Sonstige third-party funds research funding program 531/09
Further information
Period: 01.01.1900 – 30.09.2010