A new scheme for boosting in situ Fenton-like reaction in plant pathogenic tissues for selective structural degradation of capsid proteins
文献类型: 外文期刊
作者: Ma, Jun 1 ; Chen, Ming 1 ; Wang, Yujie 1 ; Li, Jiaying 3 ; Tang, Jian 1 ; Wu, Shengjun 1 ; He, Chi 4 ; Chen, J. Paul 5 ;
作者机构: 1.Chinese Acad Sci, Chongqing Inst Green & Intelligent Technol, Key Lab Reservoir Aquat Environm, Chongqing 400714, Peoples R China
2.Univ Chinese Acad Sci, Chongqing Sch, Chongqing 400714, Peoples R China
3.Yunnan Acad Agr Sci, Inst Qual Stand & Testing Technol, Kunming 650205, Peoples R China
4.Xi An Jiao Tong Univ, Sch Energy & Power Engn, State Key Lab Multiphase Flow Power Engn, Xian 710049, Shaanxi, Peoples R China
5.Natl Univ Singapore, Dept Civil & Environm Engn, 10 Kent Ridge, Singapore 117576, Singapore
6.Shenzhen Univ, Coll Chem & Environm Engn, Shenzhen 518060, Peoples R China
关键词: Internal doping; Fenton-like reactions; Plant viruses; Capsid proteins
期刊名称:JOURNAL OF NANOBIOTECHNOLOGY ( 影响因子:12.6; 五年影响因子:12.3 )
ISSN:
年卷期: 2025 年 23 卷 1 期
页码:
收录情况: SCI
摘要: Safe prevention and control of plant viruses is a global challenge. Inducing viral capsid protein (CP) degradation via hydroxyl radicals (center dot OH) generated by an in situ Fenton-like reaction within plant pathogenic tissues is proposed for combating plant viruses in this study. We designed a new Fenton-like reaction inducer, tCuinter-bCDs, which utilizes an internal doping strategy that reduces copper content by 89.89% compared to conventional doping methods, while still achieving a high coexistence of multivalent copper ions. Our research demonstrated that tCuinter-bCDs possessed functional activity to specifically recognize and proximally degrade CP. tCuinter-bCDs form complexes with CP monomers through supramolecular bonds characterized by significant electrostatic components. Within 10 min, the complex induced complete degradation of tertiary structure pockets composed of alpha-helices and beta-sheets located at residues MET1-GLU23, TYR73-ARG93, and SER147-PRO157. Based on a high-resolution 2.91 & Aring; CP model that was constructed for the first time, this degradation process is likely driven by hydrophobic interactions between tCuinter-bCDs and CP residues MET1, VAL5, THR55, and THR58, along with hydrogen bonds formed with THR4, VAL5, GLY15, PRO57, and ALA59, thereby promoting degradation of adjacent peptide segments. This represents the first study demonstrating in situ Fenton-like reactions to combat pathogens in plant systems. Our findings provide a new, efficient, and environmentally friendly approach for plant virus control.
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