17598-96-8Relevant articles and documents
Supramolecular surfactants: Polymerized bolaphiles exhibiting extraordinarily high membrane-disrupting activity
Jayasuriya, Nimal,Bosak, Stanislav,Regen, Steven L.
, p. 5851 - 5854 (1990)
Polymerized forms of saturated, olefinic, and acetylenic bolaphiles (double-headed surfactants) have been prepared by condensation of a series of α,ω-dicarboxylic acids with tridecaethylene glycol, and evaluated for their ability to induce the release of 5(6)-carboxyfluorescein (CF) entrapped within large unilamellar vesicles derived from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC). Each amphiphilic polymer was found to have substantially greater membrane-disrupting activity than that found for Triton X-100; operationally, one was more than 300 times greater in activity. Comparison of each supramolecular surfactant with its corresponding bolaphile demonstrates, in nearly all cases, that a significant enhancement in membrane-disrupting activity is provided through polymerization, and that the magnitude of this amplification decreases, exponentially, as the length of the hydrophobic segment increases. In the most striking case, the disruptive power of the supramolecular surfactant was at least 3 orders of magnitude greater than its monomeric counterpart. As one goes from saturated to olefinic to acetylenic polyesters, longer hydrophobic segments are required in order to reach a maximum in activity. From a practical standpoint, supramolecular surfactants extend nonionic detergents into a new and uncharted domain in membrane-disrupting activity.
Synthesis and analysis of polyethylene glycol linked P-glycoprotein-specific homodimers based on (-)-stipiamide
Andrus, Merritt B.,Turner, Timothy M.,Updegraff, Emily P.,Sauna, Zuben E.,Ambudkar, Suresh V.
, p. 3819 - 3822 (2007/10/03)
A series of five homodimeric polyethylene glycol (PEG) linked homodimers based on the multidrug resistance reversal agent (-)-stipiamide were made and tested for their ability to interact with P-glycoprotein, the protein responsible for multidrug resistance, using ATPase and photoaffinity displacement assays. Key reactions include a new alkoxide-mesylate displacement for the assembly of the PEG linkers and a double Sonogashira coupling reaction.
