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      https://www.ias.ac.in/article/fulltext/boms/043/0320

    • Keywords

       

      Enzymatic activity; reversible regulation; host–guest recognition; gold nanoparticle; esterase.

    • Abstract

       

      Precise and controlled regulation of enzymes is an important aspect to understand their fundamental complex biological molecular mechanism. While many synthetic receptors were developed to inhibit enzymatic activity, they lackreversible control over their function. Herein, we present an engineered nanoparticle (NP) surface that synergistically combines host–guest assembly with protein surface targeting to reversibly control enzyme activity. We demonstrate the effective inhibition of anionic esterase enzyme activity upon electrostatic binding to dimethyl-benzyl ammonium terminated positively charged gold NPs. The NP surface upon threading by non-covalent host–guest interactions with CB [7] moiety has enabled the reactivation of enzyme catalysis. This reactivation has been further reversed by disrupting NP–CB [7] complex by employing a competitive orthogonal guest, hence leading to the controlled reversibility of enzyme activity. Tuning of NP surfaces by different supramolecular interactions and concomitant protein recognition on the NP surface can thus be emphasized as a significant tool for biotechnology applications.

    • Author Affiliations

       

      MEENAKSHI PAHWA1 MANIK SHARMA1 2 SHAFEEKH KULATHINTE MEETHAL3 SARIT S AGASTI1 2 4

      1. Chemistry and Physics of Materials Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore 560064, India
      2. New Chemistry Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore 560064, India
      3. Post Graduate and Research Department of Chemistry, Pocker Sahib Memorial Orphanage College, Malappuram 676306, India
      4. School of Advanced Materials, Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore 560064, India
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