Disassembly of dendritic micellar containers due to protein binding.
Disassembling a supramolecular assembly and releasing the contents of the assembly in response to a stimulus are important goals of supramolecular chemistry. When proteins are used as the stimulus, the biological relevance of the supramolecular event dramatically increases. Although there have been efforts in which such disassembly has been achieved using enzymatic action, such events based on ligand-receptor interactions have been very limited. Here we demonstrate protein-binding-induced disassembly of dendrimer-based amphiphilic nanocontainers. We show that this disassembly is selective to the targeted protein and that the disassembly event causes a release of the sequestered guest molecules. We propose that the disassembly is caused by alteration of the hydrophilic-lipophilic balance caused by the protein binding.
Azagarsamy
Malar A
MA
Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA.
Yesilyurt
Volkan
V
Thayumanavan
S
S
D001360:Avidin / Q000737:chemistry*; D001665:Binding Sites; D001710:Biotin / Q000737:chemistry*; D050091:Dendrimers / Q000737:chemistry*; D008024:Ligands; D008823:Micelles; D008958:Models, Molecular; D015394:Molecular Structure; D010316:Particle Size; D011092:Polyethylene Glycols / Q000737:chemistry; D011485:Protein Binding
D050091:Dendrimers; D008024:Ligands; D008823:Micelles; D001360:Avidin; D011092:Polyethylene Glycols; D001710:Biotin