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Effect of detergents on the thermal behavior of elastin-like polypeptides.

Publication ,  Journal Article
Thapa, A; Han, W; Simons, RH; Chilkoti, A; Chi, EY; López, GP
Published in: Biopolymers
January 2013

Elastin-like polypeptide (ELP) fusions have been designed to allow large-scale, nonchromatographic purification of many soluble proteins by using the inverse transition cycling (ITC) method; however, the sensitivity of the aqueous lower critical solubility phase transition temperature (T(t)) of ELPs to the addition of cosolutes, including detergents, may be a potential hindrance in purification of proteins with surface hydrophobicity in such a manner. To identify detergents that are known to solubilize such proteins (e.g., membrane proteins) and that have little effect on the T(t) of the ELP, we screened a number of detergents with respect to their effects on the T(t) and secondary structures of a model ELP (denoted here as ELP180). We found that mild detergents (e.g., n-dodecyl-β-D-maltoside, Triton-X100, and 3-[(3-cholamidopropyl) dimethylamino]-1-propanesulfonate) do not alter the phase transition behavior or structure (as probed by circular dichroism) of ELP180. This result is in contrast to previous studies that showed a strong effect of other detergents (e.g., sodium dodecylsulfate) on the T(t) of ELPs. Our results clearly indicate that mild detergents do not preclude ITC-based separation of ELPs, and thus that ELP fusions may prove to be useful in the purification of detergent-solubilized recombinant hydrophobic proteins, including membrane proteins, which are otherwise notoriously difficult to extract and purify by conventional separation methods (e.g., chromatography).

Duke Scholars

Published In

Biopolymers

DOI

EISSN

1097-0282

ISSN

0006-3525

Publication Date

January 2013

Volume

99

Issue

1

Start / End Page

55 / 62

Related Subject Headings

  • Temperature
  • Solubility
  • Protein Structure, Secondary
  • Peptides
  • Models, Biological
  • Elastin
  • Detergents
  • Circular Dichroism
  • Biophysics
  • 34 Chemical sciences
 

Citation

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Thapa, A., Han, W., Simons, R. H., Chilkoti, A., Chi, E. Y., & López, G. P. (2013). Effect of detergents on the thermal behavior of elastin-like polypeptides. Biopolymers, 99(1), 55–62. https://doi.org/10.1002/bip.22137
Thapa, Arjun, Wei Han, Robin H. Simons, Ashutosh Chilkoti, Eva Y. Chi, and Gabriel P. López. “Effect of detergents on the thermal behavior of elastin-like polypeptides.Biopolymers 99, no. 1 (January 2013): 55–62. https://doi.org/10.1002/bip.22137.
Thapa A, Han W, Simons RH, Chilkoti A, Chi EY, López GP. Effect of detergents on the thermal behavior of elastin-like polypeptides. Biopolymers. 2013 Jan;99(1):55–62.
Thapa, Arjun, et al. “Effect of detergents on the thermal behavior of elastin-like polypeptides.Biopolymers, vol. 99, no. 1, Jan. 2013, pp. 55–62. Epmc, doi:10.1002/bip.22137.
Thapa A, Han W, Simons RH, Chilkoti A, Chi EY, López GP. Effect of detergents on the thermal behavior of elastin-like polypeptides. Biopolymers. 2013 Jan;99(1):55–62.
Journal cover image

Published In

Biopolymers

DOI

EISSN

1097-0282

ISSN

0006-3525

Publication Date

January 2013

Volume

99

Issue

1

Start / End Page

55 / 62

Related Subject Headings

  • Temperature
  • Solubility
  • Protein Structure, Secondary
  • Peptides
  • Models, Biological
  • Elastin
  • Detergents
  • Circular Dichroism
  • Biophysics
  • 34 Chemical sciences