Related Experiment Video
Updated: Jul 15, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
Published on: January 11, 2017
Synthesis of a multivalent chelator lipid for stably tethering histidine-tagged proteins onto membranes
1Institute of Biochemistry, Biocenter N210, Johann Wolfgang Goethe-University, Max-von-Laue Str. 9, 60438 Frankfurt am Main, Germany.
Abstract:
This protocol describes the synthesis of a lipid-like molecule carrying a head group containing two nitrilotriacetic acid moieties. This multivalent chelator lipid can be incorporated into lipid membranes, to which histidine-tagged protein can then be tethered in an oriented fashion. Possible applications of this lipid are protein tethering to solid-supported membranes, to lipid vesicles or to live cells. As compared to conventional monovalent chelator lipids, this lipid can achieve highly stable tethering of proteins by the multivalent chelator head. The eight-step synthesis described in this protocol can be completed within 4-5 weeks.
More Related Videos
Related Concept Videos
Lipids as Anchors
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Tagging and Fusion Proteins

