Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain

03 October 2018, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

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.

Keywords

intrinsically disordered protein
micelle
surfactants
self-assembly
biodegradable materials
biological materials

Supplementary materials

Title
Description
Actions
Title
Supporting Information-Klass MIcelle JACS 2018 Final
Description
Actions
Title
Complete 2Y2A Video For Paper- final
Description
Actions
Title
IDP video for paper- final
Description
Actions

Comments

Comments are not moderated before they are posted, but they can be removed by the site moderators if they are found to be in contravention of our Commenting Policy [opens in a new tab] - please read this policy before you post. Comments should be used for scholarly discussion of the content in question. You can find more information about how to use the commenting feature here [opens in a new tab] .
This site is protected by reCAPTCHA and the Google Privacy Policy [opens in a new tab] and Terms of Service [opens in a new tab] apply.