Control of supramolecular chirality of nanofibers and its effect on protein adhesion.

Abstract

Chiral nanostructure, such as the double helix of DNA and α-helix of protein, plays an important role in biochemistry and material sciences. In the organism system, the biological entities always exhibit homochirality and show preference toward one specific enantiomer. How the opposite enantiomers will affect the chirality of the supramolecular nanostructures and their interactions with the biological molecules remains an important issue. In this study, two gelators bearing amphiphilic l-glutamide and d- or l-pantolactone (abbreviated as DPLG and LPLG) were designed, and their self-assembly behavior and interactions with proteins were investigated. It was found that both of the gelators could form gels in the mixed solvent of ethanol and water, and the corresponding gels were characterized with UV-vis spectroscopy, circular dichroism, Fourier transform infrared spectroscopy, X-ray diffraction, and atomic force microscopy. Although both gels formed nanofiber structures and showed many similar properties, their supramolecular chiralities were opposite, which was determined by the chirality of the terminal group. The chirality of the nanofibrous structure is found to influence the protein adhesion significantly. Quartz crystal microbalance technique was used to investigate the adsorption of human serum albumin on the nanofibrous structures. It was revealed that supramolecular nanostructure of DPLG exhibited stronger adhesive ability than that of LPLG, while there is no clear difference at a molecular level. This suggested that slightly different interactions between d and l substances with the biological molecules could be amplified when they formed chiral nanostructures. Molecular dynamic simulations were performed to verify the interaction between the two gelators and protein molecules. A possible model was proposed to explain the interaction between the nanofibers and the proteins.