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An integrative toolbox to unlock the structure and dynamics of protein-surfactant complexes

Sanchez-Fernandez, Adrian LU orcid ; Diehl, Carl LU ; Houston, Judith E. ; Leung, Anna E. ; Tellam, James P. ; Rogers, Sarah E. ; Prevost, Sylvain ; Ulvenlund, Stefan LU ; Sjögren, Helen LU and Wahlgren, Marie LU orcid (2020) In Nanoscale Advances 2(9). p.4011-4023
Abstract

The interactions between protein and surfactants play an important role in the stability and performance of formulated products. Due to the high complexity of such interactions, multi-technique approaches are required to study these systems. Here, an integrative approach is used to investigate the various interactions in a model system composed of human growth hormone and sodium dodecyl sulfate. Contrast variation small-angle neutron scattering was used to obtain information on the structure of the protein, surfactant aggregates and surfactant-protein complexes. 1H and 1H-13C HSQC nuclear magnetic resonance spectroscopy was employed to probe the local structure and dynamics of specific amino acids upon surfactant addition. Through the... (More)

The interactions between protein and surfactants play an important role in the stability and performance of formulated products. Due to the high complexity of such interactions, multi-technique approaches are required to study these systems. Here, an integrative approach is used to investigate the various interactions in a model system composed of human growth hormone and sodium dodecyl sulfate. Contrast variation small-angle neutron scattering was used to obtain information on the structure of the protein, surfactant aggregates and surfactant-protein complexes. 1H and 1H-13C HSQC nuclear magnetic resonance spectroscopy was employed to probe the local structure and dynamics of specific amino acids upon surfactant addition. Through the combination of these advanced methods with fluorescence spectroscopy, circular dichroism and isothermal titration calorimetry, it was possible to identify the interaction mechanisms between the surfactant and the protein in the pre- and post-micellar regimes, and interconnect the results from different techniques. As such, the protein was revealed to evolve from a partially unfolded conformation at low SDS concentration to a molten globule at intermediate concentrations, where the protein conformation and local dynamics of hydrophobic amino acids are partially affected compared to the native state. At higher surfactant concentrations the local structure of the protein appears disrupted, and a decorated micelle structure is observed, where the protein is wrapped around a surfactant assembly. Importantly, this integrative approach allows for the identification of the characteristic fingerprints of complex transitions as seen by each technique, and establishes a methodology for an in-detail study of surfactant-protein systems. This journal is

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author
; ; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Nanoscale Advances
volume
2
issue
9
pages
13 pages
publisher
Royal Society of Chemistry
external identifiers
  • scopus:85093521979
ISSN
2516-0230
DOI
10.1039/d0na00194e
language
English
LU publication?
yes
id
c7b8d1a6-3632-47b5-8d2a-283fc1eca849
date added to LUP
2020-11-10 10:33:45
date last changed
2023-12-19 07:58:23
@article{c7b8d1a6-3632-47b5-8d2a-283fc1eca849,
  abstract     = {{<p>The interactions between protein and surfactants play an important role in the stability and performance of formulated products. Due to the high complexity of such interactions, multi-technique approaches are required to study these systems. Here, an integrative approach is used to investigate the various interactions in a model system composed of human growth hormone and sodium dodecyl sulfate. Contrast variation small-angle neutron scattering was used to obtain information on the structure of the protein, surfactant aggregates and surfactant-protein complexes. 1H and 1H-13C HSQC nuclear magnetic resonance spectroscopy was employed to probe the local structure and dynamics of specific amino acids upon surfactant addition. Through the combination of these advanced methods with fluorescence spectroscopy, circular dichroism and isothermal titration calorimetry, it was possible to identify the interaction mechanisms between the surfactant and the protein in the pre- and post-micellar regimes, and interconnect the results from different techniques. As such, the protein was revealed to evolve from a partially unfolded conformation at low SDS concentration to a molten globule at intermediate concentrations, where the protein conformation and local dynamics of hydrophobic amino acids are partially affected compared to the native state. At higher surfactant concentrations the local structure of the protein appears disrupted, and a decorated micelle structure is observed, where the protein is wrapped around a surfactant assembly. Importantly, this integrative approach allows for the identification of the characteristic fingerprints of complex transitions as seen by each technique, and establishes a methodology for an in-detail study of surfactant-protein systems. This journal is </p>}},
  author       = {{Sanchez-Fernandez, Adrian and Diehl, Carl and Houston, Judith E. and Leung, Anna E. and Tellam, James P. and Rogers, Sarah E. and Prevost, Sylvain and Ulvenlund, Stefan and Sjögren, Helen and Wahlgren, Marie}},
  issn         = {{2516-0230}},
  language     = {{eng}},
  number       = {{9}},
  pages        = {{4011--4023}},
  publisher    = {{Royal Society of Chemistry}},
  series       = {{Nanoscale Advances}},
  title        = {{An integrative toolbox to unlock the structure and dynamics of protein-surfactant complexes}},
  url          = {{http://dx.doi.org/10.1039/d0na00194e}},
  doi          = {{10.1039/d0na00194e}},
  volume       = {{2}},
  year         = {{2020}},
}