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Calcium binding peptide motifs from calmodulin confer divalent ion selectivity to elastin-like polypeptides.

Publication ,  Journal Article
Hassouneh, W; Nunalee, ML; Shelton, MC; Chilkoti, A
Published in: Biomacromolecules
July 2013

Calcium-sensitive elastin-like polypeptides (CELPs) were synthesized by periodically interspersing a calcium-binding peptide sequence from calmodulin within an elastin-like polypeptide (ELP) with the goal of creating thermal and calcium responsive peptide polymers. The CELPs exhibit high sensitivity to calcium compared to monovalent cations but do not exhibit the exquisite selectivity for calcium over other divalent cations, such as magnesium, that is displayed by calmodulin. The CELPs were further used as a building block for the synthesis of calcium-sensitive nanoparticles by fusing a hydrophilic, noncalcium-sensitive ELP block with a CELP block that becomes more hydrophobic upon calcium binding. We show that addition of calcium at concentrations between 50 and 500 mM imparts sufficient amphiphilicity to the diblock polypeptide between 33 and 46 °C to trigger its self-assembly into monodisperse spherical micelles with a hydrodynamic radius of ∼50 nm.

Duke Scholars

Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

July 2013

Volume

14

Issue

7

Start / End Page

2347 / 2353

Related Subject Headings

  • Surface-Active Agents
  • Polymers
  • Polymers
  • Peptides
  • Nanoparticles
  • Intracellular Calcium-Sensing Proteins
  • Hydrophobic and Hydrophilic Interactions
  • Elastin
  • Cations, Divalent
  • Calmodulin
 

Citation

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MLA
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Hassouneh, W., Nunalee, M. L., Shelton, M. C., & Chilkoti, A. (2013). Calcium binding peptide motifs from calmodulin confer divalent ion selectivity to elastin-like polypeptides. Biomacromolecules, 14(7), 2347–2353. https://doi.org/10.1021/bm400464s
Hassouneh, Wafa, Michelle L. Nunalee, M Coleman Shelton, and Ashutosh Chilkoti. “Calcium binding peptide motifs from calmodulin confer divalent ion selectivity to elastin-like polypeptides.Biomacromolecules 14, no. 7 (July 2013): 2347–53. https://doi.org/10.1021/bm400464s.
Hassouneh W, Nunalee ML, Shelton MC, Chilkoti A. Calcium binding peptide motifs from calmodulin confer divalent ion selectivity to elastin-like polypeptides. Biomacromolecules. 2013 Jul;14(7):2347–53.
Hassouneh, Wafa, et al. “Calcium binding peptide motifs from calmodulin confer divalent ion selectivity to elastin-like polypeptides.Biomacromolecules, vol. 14, no. 7, July 2013, pp. 2347–53. Epmc, doi:10.1021/bm400464s.
Hassouneh W, Nunalee ML, Shelton MC, Chilkoti A. Calcium binding peptide motifs from calmodulin confer divalent ion selectivity to elastin-like polypeptides. Biomacromolecules. 2013 Jul;14(7):2347–2353.
Journal cover image

Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

July 2013

Volume

14

Issue

7

Start / End Page

2347 / 2353

Related Subject Headings

  • Surface-Active Agents
  • Polymers
  • Polymers
  • Peptides
  • Nanoparticles
  • Intracellular Calcium-Sensing Proteins
  • Hydrophobic and Hydrophilic Interactions
  • Elastin
  • Cations, Divalent
  • Calmodulin