Journal
ANALYTICAL CHEMISTRY
Volume 86, Issue 19, Pages 9924-9929Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ac5026539
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Funding
- [2206]
- [23107514]
- [24310089]
- Grants-in-Aid for Scientific Research [25107713] Funding Source: KAKEN
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Amphiphilic tris-urea molecules self-assemble into a supramolecular hydrogel in tris(hydroxymethyl)aminomethane-glycine buffer. The supramolecular hydrogel is used as a matrix for the electrophoresis of acidic native proteins, in which proteins are separated based on their isoelectric points rather than their molecular weights. The proteins remain in their native forms during migration, and their activities are retained after electrophoresis. Glucoside substituents on the amphiphilic tris-urea molecule allow for the affinity electrophoresis of a carbohydrate-binding protein to be performed. The proteins can be efficiently recovered from the supramolecular hydrogel using a simple procedure. This is a major advantage of using this noncovalent, self-assembled material.
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