Supramolecular gel electrophoresis

Abstract

Amphiphilic C3-symmetric tris-ureas self-assemble into supramolecular hydrogels in aqueous solution. These supramolecular hydrogels were used as matrices for the electrophoresis of biopolymers such as proteins and nucleic acids. A unique separation mode in comparison to that of typical sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE) was found during the electrophoresis of denatured proteins. Native proteins were separated on the basis of their isoelectric points and retained their activities. Affinity electrophoresis was realized by exploiting interactions between gelator glucosides and carbohydrate-binding proteins. Protein samples were efficiently recovered through an extremely simple operation, and up to 50% of the protein was extracted by centrifugation, which is a remarkable feature of electrophoresis using supramolecular hydrogels. Large DNA fragments that previously had been separated only by pulsed-field gel electrophoresis were separated using a supramolecular hydrogel matrix and a typical continuous-field electrophoresis apparatus. In this focus review, the author summarizes the electrophoresis of proteins and nucleic acids using our developed supramolecular hydrogel matrix. Amphiphilic C3-symmetric tris-ureas self-assemble into supramolecular hydrogels in aqueous solution. These supramolecular hydrogels were used as matrices for the electrophoresis of biopolymers (SUGE: SupramolecularGelElectrophoresis). A unique separation mode in comparison to that of SDS–PAGE was found during the electrophoresis of denatured proteins. Native proteins were separated on the basis of their isoelectric points and retained their activities. Large DNA fragments that previously had been separated only by pulsed-field gel electrophoresis were separated using a supramolecular hydrogel matrix and a typical continuous-field electrophoresis apparatus.