Article thumbnail

Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain

By Sarah H. Klass (6401018), Matthew J. Smith (282133), Tahoe A. Fiala (6401021), Jess P. Lee (6401024), Anthony O. Omole (6401027), Bong-Gyoon Han (6401030), Kenneth H. Downing (628106), Sanjay Kumar (8853) and Matthew B. Francis (425831)


The self-assembly of micellar structures from diblock polymers that contain hydrophilic and hydrophobic domains has been of great interest for the encapsulation of drugs and other hydrophobic molecules. While most commercially used surfactants are derived from hydrocarbon sources, there have been recent efforts to replace these with biodegradable, nontoxic, biologically synthesized alternatives. Previous examples have primarily examined naturally occurring self-assembling proteins, such as silk and elastin-like sequences. 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 in the low micromolar range, 3 orders of magnitude lower than the CMC of commonly used surfactant sodium dodecyl sulfate (SDS). The reported micelles were found to solubilize hydrophobic metal complexes and organic molecules, suggesting their potential suitability for catalysis and drug delivery applications. Furthermore, the inherent flexibility in the design of these protein sequences enables the encoding of additional functionalities for many future applications. Overall, this work represents a new biomolecular alternative to traditional surfactants that are based on nonrenewable and poorly biodegradable hydrocarbon sources

Topics: Biophysics, Biochemistry, Pharmacology, Biotechnology, Evolutionary Biology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, surfactant sodium dodecyl sulfate, hydrocarbon sources, sequence, CMC, micelle, drug delivery applications, Intrinsically Disordered Protein Domain, solubilizing protein tag, SDS
Year: 2019
DOI identifier: 10.1021/jacs.8b10688.s003
OAI identifier:
Provided by: FigShare
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • (external link)
  • Suggested articles

    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.