Role of Driving Force on Engineering Layer-by-Layer Protein/Polyphenol Coating with Flexible Structures and Properties

• Published in: ACS applied materials & interfaces 2023-04, Vol.15 (16), p.20551-20562
• Main Authors: Lu, Ruofei, Zhao, Bingyang, Yang, Li, Zheng, Shengwu, Zan, Xingjie, Li, Na
• Format: Article
• Language: English
• Subjects: Antioxidants; Polyphenols; Surface Properties; Surfaces, Interfaces, and Applications; Tannins - chemistry
• ISSN: 1944-8244; 1944-8252
• DOI: 10.1021/acsami.3c02047

Protein-based coatings are of immense interest due to their rich biological functions. Layer-by-layer (LbL) assembly, as a powerful means of transferring protein functions to the material surface, has received widespread attention. However, the assembly mechanism of protein-based LbL coatings is still far from being explained, not only because of protein structure and function diversity but also characterization limitations. Herein, we monitored in situ the LbL assembly process of tannic acid (TA) and lysozyme (Lyz), a classic pair of polyphenol and protein, by combining quartz crystal microbalance with dissipation monitoring (QCM-D) and spectroscopic ellipsometry (SE). The water content, morphology, mechanical properties, antioxidant activity, and the driving force of TA-Lyz coating engineered under different pH values were analyzed in detail by various techniques. The water content, a key factor in TA-Lyz coatings, increased with increasing assembled pH values, which resulted in a porous morphology, inhomogeneous mechanical distribution, faster assembly growth, and better antioxidant activity in both acellular and cellular levels. In addition, high water content is unfavorable to both entropy and enthalpy changes, and the thermodynamic driving force of TA and Lyz assembly mainly comes from the enthalpy change brought by the noncovalent interaction between TA and Lyz. These results provide new insights into engineering the structure, function, and assembly mechanisms of protein-based coatings.