Anchoring TGF-β1 on biomaterial surface via affinitive interactions: Effects on spatial structures and bioactivity

Area of Science:

• Biomaterials Science
• Surface Chemistry
• Biotechnology

Background:

• Protein adsorption on biomaterials can lead to conformational changes, reducing bioactivity and causing adverse reactions.
• Transforming growth factor beta1 (TGF-β1) is crucial for therapeutic effects but susceptible to denaturation upon surface adsorption.

Purpose of the Study:

• To develop a peptide-grafted biopolymer surface that stabilizes the conformation of adsorbed TGF-β1.
• To investigate the impact of peptide grafting on TGF-β1 adsorption, bioactivity, and in vivo performance.

Main Methods:

• Grafting a TGF-β1-binding peptide (HSNGLPL) onto polyurethane using copper-catalyzed azide-alkyne cycloaddition (CuAAC) click chemistry.
• Characterization of the modified polymer using Fourier transform infrared spectroscopy and proton nuclear magnetic resonance spectroscopy.
• Quantification of TGF-β1 adsorption/desorption using Quartz Crystal Microbalance with Dissipation (QCM-D) monitoring.

Main Results:

• Peptide grafting was confirmed on the polyurethane surface.
• TGF-β1 adsorption on peptide-grafted surfaces resulted in a stable, less compact layer compared to unmodified polyurethane.
• In vivo studies showed accelerated immune reactions and tissue regeneration on peptide-modified polyurethane compared to controls.

Conclusions:

• Affinity-based peptide grafting effectively preserves TGF-β1 spatial conformation and bioactivity on biomaterial surfaces.
• This approach holds promise for enhancing the therapeutic efficacy of protein-loaded biomaterials and promoting tissue regeneration.