Abstract
Exploring the interaction between an azobenzene-based photoswitch and natural protein can help elucidate how the photo-control of an optical molecule participates in the transmission and delivery of proteins, as well as the effects of azo-switch trans and cis states on protein configurations. In this study, fluorescence analysis, circular dichroism spectroscopy, molecular docking, and molecular dynamics simulations were used to study the interaction among different configurations of tetra-ortho-methoxy substituted azobenzene di-maleimide (toM-ABDM), a red light-induced optical azo-switch, and lysozyme (LYZ). Results showed that toM-ABDM caused the static quenching of LYZ. The cis toM-ABDM had stronger binding affinity than trans toM-ABDM. The noncovalent interaction, hydrogen bonds and van der Waals forces, could not regulate the conformation of LYZ in photo-control. A binding model of toM-ABDM and LYZ in different forms induced by red and blue light was further established by computer simulation.
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