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Study of the interactions of proteins with a solid surface using complementary acoustic and optical techniques
Gabriela Diaconu1, Thomas Schäfer1
1POLYMAT, NanoBioSeparations Group, University of the Basque Country, Avda. Tolosa 72, 20018-San Sebastian, Spain.
Biointerphases
|July 3, 2014
Summary
Understanding protein-membrane interactions is key to controlling membrane fouling. This study reveals distinct adsorption behaviors of bovine serum albumin (BSA) and avidin on polysulfone (PSU) membranes, impacting fouling characteristics.
Area of Science:
- Materials Science
- Biotechnology
- Chemical Engineering
Background:
- Membrane-based water treatment is crucial but hindered by biofouling.
- Controlling biofouling necessitates understanding early-stage protein-membrane surface interactions.
Purpose of the Study:
- To characterize in real-time the interactions between model proteins and a polymeric membrane surface.
- To investigate the adsorbed mass, water content, and viscoelastic properties of proteins on the membrane.
Main Methods:
- Combined acoustic quartz crystal microbalance with dissipation monitoring (QCM-D) and surface plasmon resonance (SPR).
- Utilized bovine serum albumin (BSA) and avidin as model proteins.
- Employed a polysulfone (PSU) membrane as the reference surface.
Main Results:
- Both BSA and avidin irreversibly adsorbed onto the PSU surface.
- Irreversible adsorption amounts were 292 ng/cm(2) for BSA and 380 ng/cm(2) for avidin.
- BSA formed a thinner, rigid layer with 50% water content, while avidin formed a thicker, viscoelastic layer with 58% water content and greater conformational changes.
Conclusions:
- Protein adsorption characteristics significantly influence the formation and properties of the fouling layer.
- Distinct adsorption behaviors of BSA and avidin on PSU membranes offer insights into fouling mechanisms.
- Real-time characterization techniques are vital for understanding fouling initiation and developing control strategies.

