摘要
High concentrations of aldehyde-based cross-linkers have been commonly used for protein immobilization to facilitate microscale and nanoscale observations. This fixation maintains cell morphology and partial protein activity. In this study, a facile one-step strategy based on a similar concept was first developed for the bioprosthesis of a uniform core-shell gold nanorod/serum albumin (NR@SA) nanoplatform. The resultant albumin shell preserved half of its native form, leading to decreased free SA adsorption, and even these adsorbed proteins were close to their native form. This strategy efficiently prevents subsequent adsorption cascades of other proteins and has a remarkable influence on cellular uptake (of macrophages and tumor cells). Furthermore, the other, artificial part endowed NR@SAs with higher drug loading capacity and enhanced photoacoustic signal intensity for cancer theranostics compared with those of its pristine counterpart. These findings suggested that preserved fidelity and artificial characterizations provide a new perspective for biomimetic nanomaterial design.