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Unexpected multivalent display of proteins by temperature triggered self-assembly of elastin-like polypeptide block copolymers.

Publication ,  Journal Article
Hassouneh, W; Fischer, K; MacEwan, SR; Branscheid, R; Fu, CL; Liu, R; Schmidt, M; Chilkoti, A
Published in: Biomacromolecules
May 2012

We report herein the unexpected temperature triggered self-assembly of proteins fused to thermally responsive elastin-like polypeptides (ELPs) into spherical micelles. A set of six ELP block copolymers (ELP(BC)) differing in hydrophilic and hydrophobic block lengths were genetically fused to two single domain proteins, thioredoxin (Trx) and a fibronectin type III domain (Fn3) that binds the α(v)β(3) integrin. The self-assembly of these protein-ELP(BC) fusions as a function of temperature was investigated by UV spectroscopy, light scattering, and cryo-TEM. Self-assembly of the ELP(BC) was unexpectedly retained upon fusion to the two proteins, resulting in the formation of spherical micelles with a hydrodynamic radius that ranged from 24 to 37 nm, depending on the protein and ELP(BC). Cryo-TEM images confirmed the formation of spherical particles with a size that was consistent with that measured by light scattering. The bioactivity of Fn3 was retained when presented by the ELP(BC) micelles, as indicated by the enhanced uptake of the Fn3-decorated ELP(BC) micelles in comparison to the unimer by cells that overexpress the α(v)β(3) integrin. The fusion of single domain proteins to ELP(BC)s may provide a ubiquitous platform for the multivalent presentation of proteins.

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Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

May 2012

Volume

13

Issue

5

Start / End Page

1598 / 1605

Related Subject Headings

  • Tumor Cells, Cultured
  • Thioredoxins
  • Temperature
  • Polymers
  • Peptides
  • Particle Size
  • Models, Molecular
  • Micelles
  • K562 Cells
  • Hydrophobic and Hydrophilic Interactions
 

Citation

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Hassouneh, W., Fischer, K., MacEwan, S. R., Branscheid, R., Fu, C. L., Liu, R., … Chilkoti, A. (2012). Unexpected multivalent display of proteins by temperature triggered self-assembly of elastin-like polypeptide block copolymers. Biomacromolecules, 13(5), 1598–1605. https://doi.org/10.1021/bm300321n
Hassouneh, Wafa, Karl Fischer, Sarah R. MacEwan, Robert Branscheid, Chuan Lawrence Fu, Rihe Liu, Manfred Schmidt, and Ashutosh Chilkoti. “Unexpected multivalent display of proteins by temperature triggered self-assembly of elastin-like polypeptide block copolymers.Biomacromolecules 13, no. 5 (May 2012): 1598–1605. https://doi.org/10.1021/bm300321n.
Hassouneh W, Fischer K, MacEwan SR, Branscheid R, Fu CL, Liu R, et al. Unexpected multivalent display of proteins by temperature triggered self-assembly of elastin-like polypeptide block copolymers. Biomacromolecules. 2012 May;13(5):1598–605.
Hassouneh, Wafa, et al. “Unexpected multivalent display of proteins by temperature triggered self-assembly of elastin-like polypeptide block copolymers.Biomacromolecules, vol. 13, no. 5, May 2012, pp. 1598–605. Epmc, doi:10.1021/bm300321n.
Hassouneh W, Fischer K, MacEwan SR, Branscheid R, Fu CL, Liu R, Schmidt M, Chilkoti A. Unexpected multivalent display of proteins by temperature triggered self-assembly of elastin-like polypeptide block copolymers. Biomacromolecules. 2012 May;13(5):1598–1605.
Journal cover image

Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

May 2012

Volume

13

Issue

5

Start / End Page

1598 / 1605

Related Subject Headings

  • Tumor Cells, Cultured
  • Thioredoxins
  • Temperature
  • Polymers
  • Peptides
  • Particle Size
  • Models, Molecular
  • Micelles
  • K562 Cells
  • Hydrophobic and Hydrophilic Interactions