Enhancing the compatibility of the amyloid-dye hybrid nanostructure for improved photo-biocatalysis  

作　　者：Zhen Dong Yanying Wang Qin Yang Dan Li Peng Wu 

机构地区：[1]College of Chemistry,Sichuan University,Chengdu 610064,Sichuan,China [2]Analytical&Testing Centre,State Key Laboratory of Hydraulics and Mountain River Engineering,Sichuan University,Chengdu 610064,Sichuan,China [3]College of Biomass Science and Engineering,Sichuan University,Chengdu 610064,Sichuan,China [4]School of Chemistry and Chemical Engineering,Henan Normal University,Xinxiang 453007,Henan,China

出　　处：《Journal of Energy Chemistry》2023年第3期430-437,I0012,共9页能源化学（英文版）

基　　金：financial support from the National Natural Science Foundation of China(22274102 and 22001182);the Sichuan Science and Technology Program(2022ZYD0027);the Open Research Fund of School of Chemistry and Chemical Engineering,Henan Normal University(2022A02);the Fundamental Research Funds for the Central Universities。

摘　　要：Artificial photosynthesis is significant for renewable energy generation,sustainable development,and environmental protection.Dye-protein hybrids are promising for developing photosynthesis mimics(e.g.,photo-biocatalysis),but their performances are far lower than the plant photosystems,partially because of the incompatibility between dye and the protein matrix that limits excited state electron transfer of the included dyes.Here,using ThT-insulin amyloid assembly as a model system,we proposed that increasing the dye-protein compatibility could lead to the improved photo-biocatalytic performance.A ThT derivative,ThTPD,was designed with the same electron acceptor but extended π-conjugated donor structure.When integrated into the insulin amyloid,the extended π-conjugated donor structure allowed increased binding affinity and energy with the amyloid matrix,thus better electron transport to the mediator to drive the photocatalytic reaction.Meanwhile,compared with ThT, ThTPD exhibited improved light absorption and longer excited state lifetime.The photo-biocatalytic performance of ThTPD-insulin amyloid was greatly improved as compared with that of ThT in reduced nicotinamide adenine dinucleotide(NADH) regeneration.When integrating with NADH-dependent L-glutamate reductase,the efficiency of the ThTPD-insulin amyloid hybrid was 2.8-fold higher than that of ThT in glutamate generation,showing promising feature in biocatalytic solar-to-chemical conversion.

关 键 词：Photo-biocatalysis Dye-protein assembly Insulin amyloid THT Compatibility 

分 类 号：TB383.1[一般工业技术—材料科学与工程] O643.36[理学—物理化学]