[Colloid Interface Sci. Commun.] Multiplex Binding of Amyloid-like Protein Nanofilm to Different MaterialSurfaces
作者：Jin Gu, Shuting Miao, Zhigang Yan, Peng Yang*
關(guān)鍵字：Amyloid; Bioadhesion; Surface Modification; Multiplex Binding; Interfacial Bonding
論文來源：期刊
具體來源：Colloid and Interface Sci. Commun.
發(fā)表時間：2018年
The development of versatile materials and engineering devices requires multifunctional conformal coatings that give rise to immense scientific interest. With this respect, the development of a reliable universal way to form strongly bonded coating with underlying substrate independent on material chemistry is ideal surface modification strategy and remains great challenge. Recently developed polydopamine and amyloid-based adhesion systems are two representative examples reported so far to fulfill this aim, and nonetheless the universal surface adhesion mechanism in these two cases is still not unclear up to now. In order to elucidate such adhesion mechanism and design theory-driven-design novel adhesive materials, herein we studied the adhesion mechanism of amyloid-like nanofilm attached onto representative metal, inorganic and organic material surfaces, by reflection acoustic wave analysis. We constructed material-independent adhesive lysozyme nanofilm based on the recently developed amyloid-like assembly of phase-transited lysozyme (PTL). The PTL coating displayed competitive advantages over existing alternatives including controlled thickness from nano to micro-scale, colorless and optical transparency, stable bonding strength, ordered internal and surface morphology, as well as thermal/chemical stability. The systematical studies on the adhesive strength of the PTL coating on metal, organic and inorganic material surfaces reveal a novel multiplex bonding model on polar and non-polar abiotic surfaces, and different binding mode for respective material chemical structure including metal-sulfur coordination bonding, hydrogen bonding, electrostatic and hydrophobic interaction is elucidated with affirmative bonding strength. Our findings lend insight into amyloid adhesion mechanisms and reveal strategies for theory-driven design of engineered adhesives that harness great promise for advanced materials and devices.
Colloid and Interface Sci. Commun. DOI: 10.1016/j.colcom.2017.11.009.