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A unified model for de novo design of elastin-like polypeptides with tunable inverse transition temperatures.

Publication ,  Journal Article
McDaniel, JR; Radford, DC; Chilkoti, A
Published in: Biomacromolecules
August 2013

Elastin-like polypeptides (ELPs) are stimulus-responsive peptide polymers that exhibit inverse temperature phase transition behavior, causing an ELP to aggregate above its inverse transition temperature (T(t)). Although this property has been exploited in a variety of biotechnological applications, de novo design of ELPs that display a specific T(t) is not trivial because the T(t) of an ELP is a complex function of several variables, including its sequence, chain length, polypeptide concentration, and the type and concentration of cosolutes in solution. This paper provides a quantitative model that predicts the T(t) of a family of ELPs (Val-Pro-Gly-Xaa-Gly, where Xaa = Ala and/or Val) from their composition, chain length, and concentration in phosphate buffered saline. This model will enable de novo prediction of the amino acid sequence and chain length of ELPs that will display a predetermined T(t) in physiological buffer within a specified concentration regime, thereby greatly facilitating the design of new ELPs for applications in medicine and biotechnology.

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Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

August 2013

Volume

14

Issue

8

Start / End Page

2866 / 2872

Related Subject Headings

  • Transition Temperature
  • Solutions
  • Protein Engineering
  • Polymers
  • Molecular Weight
  • Models, Molecular
  • Elastin
  • Amino Acid Sequence
  • Algorithms
  • 40 Engineering
 

Citation

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McDaniel, J. R., Radford, D. C., & Chilkoti, A. (2013). A unified model for de novo design of elastin-like polypeptides with tunable inverse transition temperatures. Biomacromolecules, 14(8), 2866–2872. https://doi.org/10.1021/bm4007166
McDaniel, Jonathan R., D Christopher Radford, and Ashutosh Chilkoti. “A unified model for de novo design of elastin-like polypeptides with tunable inverse transition temperatures.Biomacromolecules 14, no. 8 (August 2013): 2866–72. https://doi.org/10.1021/bm4007166.
McDaniel JR, Radford DC, Chilkoti A. A unified model for de novo design of elastin-like polypeptides with tunable inverse transition temperatures. Biomacromolecules. 2013 Aug;14(8):2866–72.
McDaniel, Jonathan R., et al. “A unified model for de novo design of elastin-like polypeptides with tunable inverse transition temperatures.Biomacromolecules, vol. 14, no. 8, Aug. 2013, pp. 2866–72. Epmc, doi:10.1021/bm4007166.
McDaniel JR, Radford DC, Chilkoti A. A unified model for de novo design of elastin-like polypeptides with tunable inverse transition temperatures. Biomacromolecules. 2013 Aug;14(8):2866–2872.
Journal cover image

Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

August 2013

Volume

14

Issue

8

Start / End Page

2866 / 2872

Related Subject Headings

  • Transition Temperature
  • Solutions
  • Protein Engineering
  • Polymers
  • Molecular Weight
  • Models, Molecular
  • Elastin
  • Amino Acid Sequence
  • Algorithms
  • 40 Engineering