Protein Transport upon Advection at the Air/Water Interface: When Charge Matters
Coralie Pasquier1,2, Stéphane Pezennec1, Antoine Bouchoux3
1INRAE, Institut Agro, STLO, F-35042 Rennes, France.
Langmuir : the ACS Journal of Surfaces and Colloids
|October 12, 2021
Summary
Advection flow combined with positively charged proteins like lysozyme and ovalbumin can form interfacial multilayers at air-water interfaces. Negatively charged proteins form monolayers, regardless of advection.
Area of Science:
- Physical Chemistry
- Surface Science
- Biophysics
Background:
- Protein adsorption at air-water interfaces involves diffusion and advection.
- Protein interactions and interfacial layer structure depend on net charge, influenced by pH.
- The role of advection in protein adsorption kinetics and structure is not fully understood.
Purpose of the Study:
- To investigate how advection flow affects protein adsorption kinetics and interfacial layer structure.
- To determine if protein net charge (positive or negative) influences the impact of advection.
- To compare adsorption behavior of positively and negatively charged model proteins under advection and non-advection conditions.
Main Methods:
- Utilized ovalbumin and lysozyme as model proteins with varying net charges.
- Applied advection flow (water toward the interface) and controlled its absence.
- Studied interfacial layer formation and organization using neutron reflectivity and null-ellipsometry.
Main Results:
- Positively charged lysozyme and ovalbumin, with advection, formed interfacial multilayers.
- Negatively charged ovalbumin formed stable monolayers, irrespective of advection.
- Standard advection/diffusion models failed to accurately predict multilayer adsorption kinetics.
Conclusions:
- Advection flow is crucial for the formation of protein multilayers, particularly with positively charged proteins.
- Protein net charge significantly dictates whether monolayers or multilayers form under advection.
- The precise mechanism driving advection-induced multilayer formation requires further investigation.
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