title: Artificial signal transduction with primary and secondary messengers.
abstract: The complete, entirely artificial, signal-transduction process was realized with a pair of tailored transmembrane units that were equipped with receptor- and reactive sites at both amphiphilic ends. Thus, docking of the primary messenger, transmission of the signal, and release of the secondary messenger could all be imitated in a single experimental setup. The system imitates the signaling principle of receptor tyrosine kinases and employs bisphosphonate head-groups for oligoamine-recognition and a pair of thiol nucleophiles and pyridine disulfide tail-groups for intravesicle S(N)2 displacement. This system operates in a unidirectional fashion, does not suffer from intervesicle competition, and is highly sensitive towards the lipid composition of the membrane and the nature of the primary messenger.
authors.affiliation: Department of Chemistry, University of Duisburg-Essen, Universitätsstrasse 7, 45117 Essen, Germany.
authors.forename: Kai
authors.initials: K
authors.lastname: Bernitzki
authors.forename: Michael
authors.initials: M
authors.lastname: Maue
authors.forename: Thomas
authors.initials: T
authors.lastname: Schrader
mesh_terms: D015060:1,2-Dipalmitoylphosphatidylcholine / Q000737:chemistry; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry; D031541:Fluorescence Resonance Energy Transfer; D008051:Lipid Bilayers / Q000737:chemistry; D010084:Oxidation-Reduction; D011725:Pyridines / Q000737:chemistry; D015398:Signal Transduction; D013438:Sulfhydryl Compounds / Q000737:chemistry
chemical_list: D008051:Lipid Bilayers; D011725:Pyridines; D013438:Sulfhydryl Compounds; D015060:1,2-Dipalmitoylphosphatidylcholine; C023666:pyridine; D004134:Dimyristoylphosphatidylcholine