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Noncanonical self-assembly of highly asymmetric genetically encoded polypeptide amphiphiles into cylindrical micelles.

Publication ,  Journal Article
McDaniel, JR; Weitzhandler, I; Prevost, S; Vargo, KB; Appavou, M-S; Hammer, DA; Gradzielski, M; Chilkoti, A
Published in: Nano letters
November 2014

Elastin-like polypeptides (ELPs) are a class of biopolymers consisting of the pentameric repeat (VPGαG)n based on the sequence of mammalian tropoelastin that display a thermally induced soluble-to-insoluble phase transition in aqueous solution. We have discovered a remarkably simple approach to driving the spontaneous self-assembly of high molecular weight ELPs into nanostructures by genetically fusing a short 1.5 kDa (XGy)z assembly domain to one end of the ELP. Classical theories of self-assembly based on the geometric mass balance of hydrophilic and hydrophobic block copolymers suggest that these highly asymmetric polypeptides should form spherical micelles. Surprisingly, when sufficiently hydrophobic amino acids (X) are presented in a periodic sequence such as (FGG)8 or (YG)8, these highly asymmetric polypeptides self-assemble into cylindrical micelles whose length can be tuned by the sequence of the morphogenic tag. These nanostructures were characterized by light scattering, tunable resistive pulse sensing, fluorescence spectrophotometry, and thermal turbidimetry, as well as by cryogenic transmission electron microscopy (cryo-TEM) and small-angle neutron scattering (SANS). These short assembly domains provide a facile strategy to control the size, shape, and stability of stimuli responsive polypeptide nanostructures.

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Published In

Nano letters

DOI

EISSN

1530-6992

ISSN

1530-6984

Publication Date

November 2014

Volume

14

Issue

11

Start / End Page

6590 / 6598

Related Subject Headings

  • Recombinant Proteins
  • Phase Transition
  • Peptides
  • Particle Size
  • Nanostructures
  • Nanoscience & Nanotechnology
  • Molecular Sequence Data
  • Micelles
  • Hydrophobic and Hydrophilic Interactions
  • Elastin
 

Citation

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McDaniel, J. R., Weitzhandler, I., Prevost, S., Vargo, K. B., Appavou, M.-S., Hammer, D. A., … Chilkoti, A. (2014). Noncanonical self-assembly of highly asymmetric genetically encoded polypeptide amphiphiles into cylindrical micelles. Nano Letters, 14(11), 6590–6598. https://doi.org/10.1021/nl503221p
McDaniel, Jonathan R., Isaac Weitzhandler, Sylvain Prevost, Kevin B. Vargo, Marie-Sousai Appavou, Daniel A. Hammer, Michael Gradzielski, and Ashutosh Chilkoti. “Noncanonical self-assembly of highly asymmetric genetically encoded polypeptide amphiphiles into cylindrical micelles.Nano Letters 14, no. 11 (November 2014): 6590–98. https://doi.org/10.1021/nl503221p.
McDaniel JR, Weitzhandler I, Prevost S, Vargo KB, Appavou M-S, Hammer DA, et al. Noncanonical self-assembly of highly asymmetric genetically encoded polypeptide amphiphiles into cylindrical micelles. Nano letters. 2014 Nov;14(11):6590–8.
McDaniel, Jonathan R., et al. “Noncanonical self-assembly of highly asymmetric genetically encoded polypeptide amphiphiles into cylindrical micelles.Nano Letters, vol. 14, no. 11, Nov. 2014, pp. 6590–98. Epmc, doi:10.1021/nl503221p.
McDaniel JR, Weitzhandler I, Prevost S, Vargo KB, Appavou M-S, Hammer DA, Gradzielski M, Chilkoti A. Noncanonical self-assembly of highly asymmetric genetically encoded polypeptide amphiphiles into cylindrical micelles. Nano letters. 2014 Nov;14(11):6590–6598.
Journal cover image

Published In

Nano letters

DOI

EISSN

1530-6992

ISSN

1530-6984

Publication Date

November 2014

Volume

14

Issue

11

Start / End Page

6590 / 6598

Related Subject Headings

  • Recombinant Proteins
  • Phase Transition
  • Peptides
  • Particle Size
  • Nanostructures
  • Nanoscience & Nanotechnology
  • Molecular Sequence Data
  • Micelles
  • Hydrophobic and Hydrophilic Interactions
  • Elastin