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Micellar Self-Assembly of Recombinant Resilin-/Elastin-Like Block Copolypeptides.

Publication ,  Journal Article
Weitzhandler, I; Dzuricky, M; Hoffmann, I; Garcia Quiroz, F; Gradzielski, M; Chilkoti, A
Published in: Biomacromolecules
August 2017

Reported here is the synthesis of perfectly sequence defined, monodisperse diblock copolypeptides of hydrophilic elastin-like and hydrophobic resilin-like polypeptide blocks and characterization of their self-assembly as a function of structural parameters by light scattering, cryo-TEM, and small-angle neutron scattering. A subset of these diblock copolypeptides exhibit lower critical solution temperature and upper critical solution temperature phase behavior and self-assemble into spherical or cylindrical micelles. Their morphologies are dictated by their chain length, degree of hydrophilicity, and hydrophilic weight fraction of the ELP block. We find that (1) independent of the length of the corona-forming ELP block there is a minimum threshold in the length of the RLP block below which self-assembly does not occur, but that once that threshold is crossed, (2) the RLP block length is a unique molecular parameter to independently tune self-assembly and (3) increasing the hydrophobicity of the corona-forming ELP drives a transition from spherical to cylindrical morphology. Unlike the self-assembly of purely ELP-based block copolymers, the self-assembly of RLP-ELPs can be understood by simple principles of polymer physics relating hydrophilic weight fraction and polymer-polymer and polymer-solvent interactions to micellar morphology, which is important as it provides a route for the de novo design of desired nanoscale morphologies from first principles.

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Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

August 2017

Volume

18

Issue

8

Start / End Page

2419 / 2426

Related Subject Headings

  • Scattering, Small Angle
  • Recombinant Fusion Proteins
  • Polymers
  • Neutron Diffraction
  • Micelles
  • Insect Proteins
  • Escherichia coli
  • Elastin
  • 40 Engineering
  • 34 Chemical sciences
 

Citation

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ICMJE
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Weitzhandler, I., Dzuricky, M., Hoffmann, I., Garcia Quiroz, F., Gradzielski, M., & Chilkoti, A. (2017). Micellar Self-Assembly of Recombinant Resilin-/Elastin-Like Block Copolypeptides. Biomacromolecules, 18(8), 2419–2426. https://doi.org/10.1021/acs.biomac.7b00589
Weitzhandler, Isaac, Michael Dzuricky, Ingo Hoffmann, Felipe Garcia Quiroz, Michael Gradzielski, and Ashutosh Chilkoti. “Micellar Self-Assembly of Recombinant Resilin-/Elastin-Like Block Copolypeptides.Biomacromolecules 18, no. 8 (August 2017): 2419–26. https://doi.org/10.1021/acs.biomac.7b00589.
Weitzhandler I, Dzuricky M, Hoffmann I, Garcia Quiroz F, Gradzielski M, Chilkoti A. Micellar Self-Assembly of Recombinant Resilin-/Elastin-Like Block Copolypeptides. Biomacromolecules. 2017 Aug;18(8):2419–26.
Weitzhandler, Isaac, et al. “Micellar Self-Assembly of Recombinant Resilin-/Elastin-Like Block Copolypeptides.Biomacromolecules, vol. 18, no. 8, Aug. 2017, pp. 2419–26. Epmc, doi:10.1021/acs.biomac.7b00589.
Weitzhandler I, Dzuricky M, Hoffmann I, Garcia Quiroz F, Gradzielski M, Chilkoti A. Micellar Self-Assembly of Recombinant Resilin-/Elastin-Like Block Copolypeptides. Biomacromolecules. 2017 Aug;18(8):2419–2426.
Journal cover image

Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

August 2017

Volume

18

Issue

8

Start / End Page

2419 / 2426

Related Subject Headings

  • Scattering, Small Angle
  • Recombinant Fusion Proteins
  • Polymers
  • Neutron Diffraction
  • Micelles
  • Insect Proteins
  • Escherichia coli
  • Elastin
  • 40 Engineering
  • 34 Chemical sciences