Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain
Keyword(s):
Herein, we describe a new series of fusion proteins that have been developed to self-assemble spontaneously into stable micelles that are 27 nm in diameter after enzymatic cleavage of a solubilizing protein tag. The sequences of the proteins are based on a human intrinsically disordered protein, which has been appended with a hydrophobic segment. The micelles were found to form across a broad range of pH, ionic strength, and temperature conditions, with critical micelle concentration (CMC) values below 1 µM being observed in some cases. The reported micelles were found to solubilize hydrophobic metal complexes and organic molecules, suggesting their potential suitability for catalysis and drug delivery applications.
2018 ◽
2019 ◽
Vol 141
(10)
◽
pp. 4291-4299
◽
2013 ◽
Vol 14
(7)
◽
pp. 13282-13306
◽
2018 ◽
Vol 13
(5)
◽
pp. 1218-1227
◽
2021 ◽
Vol 168
◽
pp. 1-12