Self-Assembling Protein-Polymer Bioconjugates for Surfaces with Antifouling Features and Low Nonspecific Binding

Area of Science:

• Materials Science
• Surface Chemistry
• Biotechnology

Background:

• Developing antifouling and low-adsorption surfaces is crucial for various applications, including biosensors and medical devices.
• Traditional methods often require harsh pretreatments, limiting their applicability to sensitive substrates.
• Hydrophobic substrates pose challenges for surface modification due to their low reactivity.

Purpose of the Study:

• To develop an energy-efficient and environmentally friendly method for creating antifouling and low nonspecific adsorption surfaces.
• To functionalize poorly reactive hydrophobic substrates without aggressive pre-treatments.
• To create surfaces capable of specific protein binding with minimal background adsorption.

Main Methods:

• Covalent modification of hydrophobin with a polymerization initiator.
• Self-assembly of hydrophobin monolayer on hydrophobic surfaces.
• In situ surface-initiated polymerization of poly(ethylene glycol) methyl ether acrylate (PEGA) using Cu(0)-mediated living radical polymerization.
• Immobilization of Protein A for IgG1 binding.

Main Results:

• Successful preparation of antifouling surfaces on hydrophobic substrates.
• Demonstrated significant reduction in nonspecific adsorption.
• Achieved specific IgG1 binding through immobilized Protein A.
• Characterization confirmed surface modification via contact angle, XPS, and AFM; antifouling and low nonspecific binding verified by QCM-D.

Conclusions:

• The developed method provides an effective strategy for creating advanced functional surfaces on hydrophobic materials.
• This approach offers a versatile platform for applications requiring specific biomolecule capture and resistance to fouling.
• The combination of hydrophobins and surface-initiated polymerization presents a promising route for next-generation biomaterials.