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The Amphoteric Surfactant N,N-Dimethyldodecylamine N-Oxide Unfolds ß-Lactoglobulin above the Critical Micelle Concentration.
Thompson, Kayla D; Danielson, Evan P; Peterson, Kerri N; Nocevski, Nicholas O; Boock, Jason T; Berberich, Jason A.
Afiliación
  • Thompson KD; Department of Chemical, Paper, and Biomedical Engineering, Miami University, Oxford, Ohio 45056, United States.
  • Danielson EP; Department of Chemical, Paper, and Biomedical Engineering, Miami University, Oxford, Ohio 45056, United States.
  • Peterson KN; Department of Chemical, Paper, and Biomedical Engineering, Miami University, Oxford, Ohio 45056, United States.
  • Nocevski NO; Department of Chemical, Paper, and Biomedical Engineering, Miami University, Oxford, Ohio 45056, United States.
  • Boock JT; Department of Chemical, Paper, and Biomedical Engineering, Miami University, Oxford, Ohio 45056, United States.
  • Berberich JA; Department of Chemical, Paper, and Biomedical Engineering, Miami University, Oxford, Ohio 45056, United States.
Langmuir ; 38(13): 4090-4101, 2022 04 05.
Article en En | MEDLINE | ID: mdl-35325533
Understanding the interactions between surfactants and proteins is important for the formulation of consumer products as surfactant binding can alter protein activity and stability. Additionally, the structure of the protein-surfactant complex can influence surface activity, which is important for emulsion and foam development. N,N-Dimethyldodecylamine N-oxide (DDAO) is an amphoteric surfactant that is nonionic at high pH. It is often used as a foam booster in detergent formulations and for the extraction of membrane proteins. In this study, a variety of biophysical characterization methods was used to investigate the impact of DDAO at pH 8 on the structure of the globular protein ß-lactoglobulin (ßLG). Pyrene fluorescence and surface tension studies show that ßLG had minimal impact on the critical micelle concentration (CMC) of DDAO, while fluorescence and circular dichroism spectroscopy found unfolding of ßLG at concentrations of DDAO greater than the CMC. Small-angle X-ray scattering results confirm changes in the structure of ßLG at DDAO concentrations above the CMC. Taken together, DDAO behaves like nonionic and zwitterionic surfactants below its CMC with limited interaction with ßLG, while it induces protein unfolding at concentrations higher than the CMC, resulting in a protein-surfactant complex structure that resembles a protein-decorated micelle.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tensoactivos / Lactoglobulinas Idioma: En Revista: Langmuir Asunto de la revista: QUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tensoactivos / Lactoglobulinas Idioma: En Revista: Langmuir Asunto de la revista: QUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos