Secondary Structure-Dominated Layer-by-Layer Growth Mode of Protein Coatings.

ABSTRACT

Benefiting from the luxury functions of proteins, protein coatings have been extended to various applications, including tissue engineering scaffolds, drug delivery, antimicrobials, sensing and diagnostic equipment, food packaging, etc. Fast construction of protein coatings is always interesting to materials science and significant to industrialization. Here, we report a layer-by-layer (LbL) multilayer-constructed coating of tannic acid (TA) and lysozyme (Lyz), in which the secondary conformations of Lyz dominate the growth rate of the TA/Lyz coating. As well characterized by various techniques (quartz crystal microbalance with dissipation (QCM-D), circular dichroism (CD) spectra, Fourier transform infrared (FTIR) spectroscopy, atomic force microscopy (AFM), contact angle, etc.), TA-induced conformational transition of Lyz to α-helices occurs at pH 8 from other secondary structures (ß-sheets, ß-turns, and random coils), which leads to the very fast growth of TA/Lyz with a number of deposited bilayers, with thicknesses of more than 90 nm for six bilayers. In contrast to the leading conformation of α-helices at pH 8, Lyz displayed multiple conformations (α-helices, ß-sheets, ß-turns, and random coils) at pH 6, which resulted in coating thicknesses of less than 30 nm for six bilayers. By the addition of NaCl, Tween 20, and urea, we further confirmed that the secondary conformations of Lyz relied greatly on the interactions between TA and Lyz and dominated the growth rate of the multilayers. We believe that these findings will help to understand the transformation of secondary conformations by TA or other polyphenols and inspire a new route to quickly build protein coatings.