Nonfouling Coatings from Synthetic Intrinsically Disordered Proteins

Area of Science:

• Biomaterials Science
• Surface Chemistry
• Protein Engineering

Background:

• Antifouling coatings are crucial for preventing unwanted surface interactions.
• Existing synthetic polymers and small molecules have limitations in performance and biocompatibility.
• Triblock proteins offer a potential platform for developing advanced biomaterials.

Purpose of the Study:

• To optimize the antifouling performance of a previously developed B-M-E triblock protein.
• To engineer a nonfouling protein layer on gold surfaces by modifying the E block sequence.
• To evaluate the performance of the optimized B-M-E protein as a robust antifouling coating.

Main Methods:

• Screening of intrinsically disordered proteins (IDPs) for nonfouling properties.
• Modification of the E block in the B-M-E protein with a selected IDP sequence: [(GAGAIP)3-(GAGEIP)]4.
• Self-assembly of the modified B-M-E protein onto gold surfaces to form protein brushes.
• Characterization of the nonfouling performance and bacterial resistance of the protein coating.

Main Results:

• An optimized B-M-E protein with an E block sequence of [(GAGAIP)3-(GAGEIP)]4 was developed.
• The resulting B-M-E protein brushes formed a nonfouling layer on gold surfaces.
• The antifouling performance was comparable to self-assembled monolayers (SAMs) of tetraethylene glycol-terminated alkanethiols.
• The protein-coated gold surfaces demonstrated resistance to E. coli attachment for at least seven days.

Conclusions:

• The engineered B-M-E protein provides an effective and scalable nonfouling coating for gold surfaces.
• This protein-based coating offers a robust alternative to conventional synthetic antifouling materials.
• The study highlights the potential of intrinsically disordered proteins in biomaterial design for surface functionalization.