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Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain

submitted on 02.10.2018, 17:20 and posted on 03.10.2018, 13:09 by Sarah Klass, Matthew J. Smith, Tahoe Fiala, Jessica Lee, Anthony Omole, Kenneth Downing, Matthew Francis
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.


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University of California Berkeley


United States of America

ORCID For Submitting Author


Declaration of Conflict of Interest

a provisional patent on this material has been submitted