title: Redox control of GPx catalytic activity through mediating self-assembly of Fmoc-phenylalanine selenide into switchable supramolecular architectures.
abstract: Artificial enzymes capable of achieving tunable catalytic activity through stimuli control of enzymatic structure transition are of significance in biosensor and biomedicine research. Herein we report a novel smart glutathione peroxidise (GPx) mimic with modulatory catalytic activity based on redox-induced supramolecular self-assembly. First, an amphiphilic Fmoc-phenylalanine-based selenide was designed and synthesized, which can self-assemble into nanospheres (NSs) in aqueous solution. The NSs demonstrate extremely low GPx activity. Upon the oxidation of hydroperoxides (ROOH), the selenide can be quickly transformed into the selenoxide form. The change of the molecular structure induces complete morphology transition of the self-assemblies from NSs to nanotubes (NTs), resulting in great enhancement in the GPx catalytic activity. Under the reduction of GSH, the selenoxide can be further reversibly reduced back into the selenide; therefore the reversible switch between the NSs and NTs can be successfully accomplished. The relationship between the catalytic activity and enzymatic structure was also investigated. The dual response nature makes this mimic play roles of both a sensor and a GPx enzyme at the same time, which can auto-detect the signal of ROOH and then auto-change its activity to achieve quick or slow/no scavenging of ROOH. The dynamic balance of ROOH is vital in organisms, in which an appropriate amount of ROOH does benefit to the metabolism, whereas surplus ROOH can cause oxidative damage of the cell instead and this smart mimic is of remarkable significance. We expect that such a mimic can be developed into an effective antioxidant drug and provide a new platform for the construction of intelligent artificial enzymes with multiple desirable properties.
authors.affiliation: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun 130012, People's Republic of China. junqiuliu@jlu.edu.cn zdong@jlu.edu.cn.
authors.forename: Zupeng
authors.initials: Z
authors.lastname: Huang
authors.forename: Quan
authors.initials: Q
authors.lastname: Luo
authors.forename: Shuwen
authors.initials: S
authors.lastname: Guan
authors.forename: Jianxiong
authors.initials: J
authors.lastname: Gao
authors.forename: Yongguo
authors.initials: Y
authors.lastname: Wang
authors.forename: Bo
authors.initials: B
authors.lastname: Zhang
authors.forename: Liang
authors.initials: L
authors.lastname: Wang
authors.forename: Jiayun
authors.initials: J
authors.lastname: Xu
authors.forename: Zeyuan
authors.initials: Z
authors.lastname: Dong
authors.forename: Junqiu
authors.initials: J
authors.lastname: Liu
mesh_terms: D040761:Biomimetic Materials / Q000737:chemistry*; D005979:Glutathione Peroxidase / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry; D054118:Nanospheres / Q000737:chemistry*; D016566:Organoselenium Compounds / Q000737:chemistry*; D010084:Oxidation-Reduction; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry; D018036:Selenium Compounds / Q000737:chemistry
chemical_list: D016566:Organoselenium Compounds; D018036:Selenium Compounds; D010649:Phenylalanine; D006861:Hydrogen Peroxide; D005979:Glutathione Peroxidase