A cytochrome c-urea functionalized dipeptide conjugate: an efficient HBD framework to synthesize 4H-pyrans via one-pot multicomponent reaction
This work is focused on the development of an efficient and green protocol for the one-pot multicomponent synthesis of a series of 4H-pyran derivatives. Herein, a protein-peptide conjugate (SS1-Cyt. c) is synthesized and characterized using Circular Dichroism (CD), UV-Visible absorption spectroscopy...
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Veröffentlicht in: | Green chemistry : an international journal and green chemistry resource : GC 2020-01, Vol.22 (3), p.956-968 |
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Sprache: | eng |
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Zusammenfassung: | This work is focused on the development of an efficient and green protocol for the one-pot multicomponent synthesis of a series of 4H-pyran derivatives. Herein, a protein-peptide conjugate (SS1-Cyt. c) is synthesized and characterized using Circular Dichroism (CD), UV-Visible absorption spectroscopy, and docking studies. The whole assembly is used as an efficient catalytic system by incorporating a derivatized dipeptide molecule in the hydrophobic cavities of the protein Cytochrome c (Cyt. c) that leads to the activation of Hydrogen Bond Donating (HBD) units of a urea derivative of a dipeptide (SS1). The HBD units tend to show non-covalent interactions with the reactant species responsible for triggering the occurrence of an organic transformation. Also, the stability and binding interactions of SS1-Cyt. c with the multicomponent reactants involved in the organic transformation are studied in detail using MD-simulation studies. It is a metal-free catalyst and provides higher yield in relatively short reaction times. As per green chemistry principles, the catalyst has provided us ideal Eco-scale and E factor scores of 79 and 0.089, respectively. |
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ISSN: | 1463-9262 1463-9270 |
DOI: | 10.1039/c9gc03512e |