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Elastin-like polypeptides as models of intrinsically disordered proteins.

Publication ,  Journal Article
Roberts, S; Dzuricky, M; Chilkoti, A
Published in: FEBS letters
September 2015

Elastin-like polypeptides (ELPs) are a class of stimuli-responsive biopolymers inspired by the intrinsically disordered domains of tropoelastin that are composed of repeats of the VPGXG pentapeptide motif, where X is a "guest residue". They undergo a reversible, thermally triggered lower critical solution temperature (LCST) phase transition, which has been utilized for a variety of applications including protein purification, affinity capture, immunoassays, and drug delivery. ELPs have been extensively studied as protein polymers and as biomaterials, but their relationship to other disordered proteins has heretofore not been established. The biophysical properties of ELPs that lend them their unique material behavior are similar to the properties of many intrinsically disordered proteins (IDP). Their low sequence complexity, phase behavior, and elastic properties make them an interesting "minimal" artificial IDP, and the study of ELPs can hence provide insights into the behavior of other more complex IDPs. Motivated by this emerging realization of the similarities between ELPs and IDPs, this review discusses the biophysical properties of ELPs, their biomedical utility, and their relationship to other disordered polypeptide sequences.

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Published In

FEBS letters

DOI

EISSN

1873-3468

ISSN

0014-5793

Publication Date

September 2015

Volume

589

Issue

19 Pt A

Start / End Page

2477 / 2486

Related Subject Headings

  • Transition Temperature
  • Protein Conformation
  • Peptides
  • Models, Molecular
  • Models, Chemical
  • Intrinsically Disordered Proteins
  • Hydrophobic and Hydrophilic Interactions
  • Humans
  • Elastin
  • Biochemistry & Molecular Biology
 

Citation

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Roberts, S., Dzuricky, M., & Chilkoti, A. (2015). Elastin-like polypeptides as models of intrinsically disordered proteins. FEBS Letters, 589(19 Pt A), 2477–2486. https://doi.org/10.1016/j.febslet.2015.08.029
Roberts, Stefan, Michael Dzuricky, and Ashutosh Chilkoti. “Elastin-like polypeptides as models of intrinsically disordered proteins.FEBS Letters 589, no. 19 Pt A (September 2015): 2477–86. https://doi.org/10.1016/j.febslet.2015.08.029.
Roberts S, Dzuricky M, Chilkoti A. Elastin-like polypeptides as models of intrinsically disordered proteins. FEBS letters. 2015 Sep;589(19 Pt A):2477–86.
Roberts, Stefan, et al. “Elastin-like polypeptides as models of intrinsically disordered proteins.FEBS Letters, vol. 589, no. 19 Pt A, Sept. 2015, pp. 2477–86. Epmc, doi:10.1016/j.febslet.2015.08.029.
Roberts S, Dzuricky M, Chilkoti A. Elastin-like polypeptides as models of intrinsically disordered proteins. FEBS letters. 2015 Sep;589(19 Pt A):2477–2486.
Journal cover image

Published In

FEBS letters

DOI

EISSN

1873-3468

ISSN

0014-5793

Publication Date

September 2015

Volume

589

Issue

19 Pt A

Start / End Page

2477 / 2486

Related Subject Headings

  • Transition Temperature
  • Protein Conformation
  • Peptides
  • Models, Molecular
  • Models, Chemical
  • Intrinsically Disordered Proteins
  • Hydrophobic and Hydrophilic Interactions
  • Humans
  • Elastin
  • Biochemistry & Molecular Biology