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Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain

preprint
submitted on 02.10.2018 and posted on 03.10.2018 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.

History

Email Address of Submitting Author

mbfrancis@berkeley.edu

Institution

University of California Berkeley

Country

United States of America

ORCID For Submitting Author

0000-0003-2837-2538

Declaration of Conflict of Interest

a provisional patent on this material has been submitted

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