▎ 摘　　要

Graphene oxide (GO) are subjected to photoaging in aquatic environment, and inevitably enter biota and then interact with proteins. Here, the interactions of pristine and photoaged GO with two typical proteins (bovine serum albumin (BSA) and lysozyme) were systematically investigated. Due to long term photoirradiation (1-3 day), the lateral size of GO decreased greatly, and the oxygen-containing groups decreased as well while the graphitic carbon contents increased. Compared to pristine GO, the photoaged GO displayed stronger binding affinities with both proteins, which was mainly attributed to the increased binding sites as a result of smaller lateral size and increased hydrophobicity. The photoaging effect was more obvious for the negatively charged BSA, because hydrogen bonding and van der Waals force were mainly involved in the enthalpy-driven interactions between them. While, the strong electrostatic attraction between the positively charged lysozyme and GO diminished the photoaging effect. Analyses of synchronous, three-dimensional fluorescence spectra and fibrillation experiments intensified that the photoaged GO induced more serious changes in conformational structure of BSA and exhibited stronger inhibition on fibrillation of BSA compared to pristine GO. This study provided novel insights into the increased ecological risks of GO as a result of photoaging.