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AgAu-modified quasi-MIL-53 hybrid nanozymes with triple enzyme-like activities for boosting biocatalytic disinfection.
Zhong, Sheng; Mo, Fayin; Chen, Linxi; Qin, Weiwei; Zhang, Luyong; Lu, Jing; Sun, Duanping.
Afiliação
  • Zhong S; Guangdong Provincial Key Laboratory of Pharmaceutical Bioactive Substances, Key Specialty of Clinical Pharmacy, The First Affiliated Hospital, Center for Drug Research and Development, Guangdong Pharmaceutical University, Guangzhou 510006, Guangdong, China.
  • Mo F; Guangdong Provincial Key Laboratory of Pharmaceutical Bioactive Substances, Key Specialty of Clinical Pharmacy, The First Affiliated Hospital, Center for Drug Research and Development, Guangdong Pharmaceutical University, Guangzhou 510006, Guangdong, China.
  • Chen L; Guangdong Provincial Key Laboratory of Pharmaceutical Bioactive Substances, Key Specialty of Clinical Pharmacy, The First Affiliated Hospital, Center for Drug Research and Development, Guangdong Pharmaceutical University, Guangzhou 510006, Guangdong, China.
  • Qin W; Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, College of Life Sciences, China Jiliang University, Hangzhou 310018, Zhejiang, China.
  • Zhang L; Guangdong Provincial Key Laboratory of Pharmaceutical Bioactive Substances, Key Specialty of Clinical Pharmacy, The First Affiliated Hospital, Center for Drug Research and Development, Guangdong Pharmaceutical University, Guangzhou 510006, Guangdong, China. Electronic address: lyzhang@gdpu.edu.cn.
  • Lu J; National and Local United Engineering Lab of Druggability and New Drugs Evaluation, School of Pharmaceutical Sciences, Sun Yat-Sen University, Guangzhou 510006, Guangdong, China. Electronic address: lujing28@mail.sysu.edu.cn.
  • Sun D; Guangdong Provincial Key Laboratory of Pharmaceutical Bioactive Substances, Key Specialty of Clinical Pharmacy, The First Affiliated Hospital, Center for Drug Research and Development, Guangdong Pharmaceutical University, Guangzhou 510006, Guangdong, China. Electronic address: sundp@gdpu.edu.cn.
J Colloid Interface Sci ; 661: 520-532, 2024 May.
Article em En | MEDLINE | ID: mdl-38308892
ABSTRACT
Metal-organic frameworks (MOFs) have great potential for combating pathogenic bacterial infections and are expected to become an alternative to antibiotics. However, organic linkers obstruct and saturate the inorganic nodes of MOF structures, making it challenging to utilize the applied potential of metal centers. Here, we combined controlled ligand decarboxylation with noble metal nanoparticles to rationally remodel MIL-53, resulting in a hybrid nanozyme (AgAu@QMIL-53, AAQM) with excellent multiple enzyme-like activities that both eradicate bacteria and promote diabetic wound healing. Specifically, benefitting from oxidase (OXD)-like and peroxidase (POD)-like activities, AAQM converts oxygen (O2) and hydrogen peroxide (H2O2) into superoxide anion radicals (O2-) and hydroxyl radicals (OH) to eradicate bacteria. In in vitro antibacterial experiments, AAQM exhibited favorable killing efficacy against Pseudomonas aeruginosa (P. aeruginosa) and methicillin-resistant Staphylococcus aureus (MRSA) (>99 %). Notably, due to its superoxide (SOD)-like activity and outstanding reactive nitrogen species (RNS) elimination capacity, AAQM can produce adequate O2 and alleviate oxidative stress in diabetic wounds. Benefiting from the rational modification of MIL-53, the synthesized hybrid nanozyme can effectively kill bacteria while alleviating oxidative stress and ultimately promote infected diabetic wound healing. Overall, this biomimetic enzyme-catalyzed strategy will bring enlightenment to the design of self-antibacterial agents for efficient disinfection and wound healing simultaneously.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Diabetes Mellitus / Staphylococcus aureus Resistente à Meticilina Limite: Humans Idioma: En Revista: J Colloid Interface Sci Ano de publicação: 2024 Tipo de documento: Article País de afiliação: China

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Diabetes Mellitus / Staphylococcus aureus Resistente à Meticilina Limite: Humans Idioma: En Revista: J Colloid Interface Sci Ano de publicação: 2024 Tipo de documento: Article País de afiliação: China