▎ 摘　　要

The fragment of viral protein R (Vpr), Vpr13-33, plays an important role in regulating nuclear importing of HIV through ion channel formation with a leucine-zipper-like a-helical conformation. Herein we report an approach to reduce cytotoxicity of Vpr13-33 by graphene oxide induced conformation change and aggregation. Preferential adsorption of Vpr13-33 on graphene oxide accompanied by conformation change from a-helix to beta-sheet structures has been observed by using atomic force microscopy (AFM) and circular dichroism (CD). The submolecular structures of the Vpr13-33 peptide assembly on graphite surface have been identified by using scanning tunneling microscopy (STM), which confirms the beta-sheet structures of Vpr13-33 on graphene oxide surface. The reduced cytotoxicity of Vpr13-33 to neuroblastoma cells and T cells are detected by MTT assay, which could be associated with the conformation change and stimulated aggregation of Vpr13-33 upon addition of graphene oxide through hydrophobic interaction. Furthermore, fluorescent leakage assay by using large unilamellar vesicles (LUVs) indicated that the GO reduced Vpr13-33-induced cytotoxicity could be associated with the inhibited "pore forming" function of Vpr13-33 by conformation change and aggregation. (C) 2012 Elsevier Ltd. All rights reserved.