1. Allosteric Modulation for Widely Spread Orthologous Tyrosinase Enzyme by Short Peptidyl-Urea Analogue: Facile Syntheses of Spiro Compounds.
- Author
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Saini, Sanjeev, Kaur, Kamalpreet, Mayank, Kaur, Navneet, and Singh, Narinder
- Subjects
SPIRO compounds synthesis ,ALLOSTERIC regulation ,PHENOL oxidase ,NUCLEAR magnetic resonance ,ENZYMES ,CIRCULAR dichroism - Abstract
The present work demonstrates the development of an efficient catalytic hybrid model (Tyr-SS2) to synthesize various spiro-oxindoles derivatives. We have designed and synthesized a functionalized dipeptide molecule (SS2) that acts as an allosteric modulator by incorporating itself into the binding cavity of the widely spread orthologous tyrosinase enzyme (Tyr). The allosterically modified Tyr-SS2 hybrid is thoroughly characterized by using various spectroscopic techniques. Its structural stability and reusability were ensured using various analytical techniques viz. Circular Dichroism (CD), Nuclear Magnetic Resonance (NMR), Fluorescence, and UV–Visible absorption spectroscopy. The Tyr-SS2 hybrid complex was used as a catalyst for the synthesis of a series of Spiro-oxindoles derivatives, and the final products obtained were characterized by NMR and High-Resolution Mass Spectrometry (HRMS) techniques. The interactions within the Tyr-SS2 complex, the catalytic mechanism, and binding interactions between the reactants and Tyr-SS2 hybrid complex were investigated extensively by molecular docking and MD-Simulation studies. Green scale parameters like Eco scale and E-factor calculations, found to be 80 and 0.096, respectively, are the key features of the current work. Allosteric modulation of tyrosinase enzyme was achieved by incorporating functionalized dipeptide in its binding cavity and used it as hybrid catalytic assembly for the facile synthesis of spiro-oxindoles in good (%) yield. [ABSTRACT FROM AUTHOR]
- Published
- 2024
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