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Synthesis and characterization of new 4H-chromene-3-carboxylates ensuring potent elastase inhibition activity along with their molecular docking and chemoinformatics properties.
Bioorg Chem. 2020 Jul; 100:103906.BC

Abstract

A new series of 4H-chromene-3-carboxylate derivatives were synthesized using multicomponent reaction of salicylaldehyde, ethyl acetoacetate and dimedone in ethanol with K3PO4 as a catalyst at 80 °C. The structures of all newly synthesized compounds were confirmed by spectral techniques viz. IR, 1H NMR, 13C NMR, and LCMS analysis. The newly synthesized compounds 4a to 4j were screened against elastase enzyme. Interestingly, all these compounds found to be potent elastase inhibitors with much lower IC50 value. The compound 4b was found to be most potent elastase inhibitor (IC50 = 0.41 ± 0.01 µM) amongst the synthesized series against standard Oleanolic Acid (IC50 value = 13.45 ± 0.0 µM). The Kinetics mechanism for compound 4b was analyzed by Lineweaver-Burk plots which revealed that compound inhibited elastase competitively by forming an enzyme-inhibitor complex. Along with this, all the synthesized compounds (4a - 4j) exhibits excellent DPPH free radical scavenging ability. The inhibition constant Ki for compound 4b was found to be 0.6 µM. The computational study was comprehensible with the experimental results with good docking energy values (Kcal/mol). Therefore, these molecules can be considered as promising medicinal scaffolds for the treatment of skin-related maladies.

Authors+Show Affiliations

Department of Biological Sciences, Kongju National University, Gongju, Chungnam 32588, Republic of Korea.Department of Chemistry, Kongju National University, Gongju, Chungnam 32588, Republic of Korea.Department of Biological Sciences, Kongju National University, Gongju, Chungnam 32588, Republic of Korea.Institute of Molecular Biology and Biotechnology, The University of Lahore, Defence road, Lahore 54590, Pakistan.Department of Chemistry, Kongju National University, Gongju, Chungnam 32588, Republic of Korea.Department of Biological Sciences, Kongju National University, Gongju, Chungnam 32588, Republic of Korea.Department of Chemistry, Kongju National University, Gongju, Chungnam 32588, Republic of Korea.School of Chemical Sciences and Food Technology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia (UKM), 43600 Bangi, Selangor, Malaysia. Electronic address: jalifah@ukm.edu.my.Department of Biological Sciences, Kongju National University, Gongju, Chungnam 32588, Republic of Korea. Electronic address: dnalove@kongju.ac.kr.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32422387

Citation

Dige, Nilam C., et al. "Synthesis and Characterization of New 4H-chromene-3-carboxylates Ensuring Potent Elastase Inhibition Activity Along With Their Molecular Docking and Chemoinformatics Properties." Bioorganic Chemistry, vol. 100, 2020, p. 103906.
Dige NC, Mahajan PG, Raza H, et al. Synthesis and characterization of new 4H-chromene-3-carboxylates ensuring potent elastase inhibition activity along with their molecular docking and chemoinformatics properties. Bioorg Chem. 2020;100:103906.
Dige, N. C., Mahajan, P. G., Raza, H., Hassan, M., Vanjare, B. D., Hong, H., Lee, K. H., Latip, J., & Seo, S. Y. (2020). Synthesis and characterization of new 4H-chromene-3-carboxylates ensuring potent elastase inhibition activity along with their molecular docking and chemoinformatics properties. Bioorganic Chemistry, 100, 103906. https://doi.org/10.1016/j.bioorg.2020.103906
Dige NC, et al. Synthesis and Characterization of New 4H-chromene-3-carboxylates Ensuring Potent Elastase Inhibition Activity Along With Their Molecular Docking and Chemoinformatics Properties. Bioorg Chem. 2020;100:103906. PubMed PMID: 32422387.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Synthesis and characterization of new 4H-chromene-3-carboxylates ensuring potent elastase inhibition activity along with their molecular docking and chemoinformatics properties. AU - Dige,Nilam C, AU - Mahajan,Prasad G, AU - Raza,Hussain, AU - Hassan,Mubashir, AU - Vanjare,Balasaheb D, AU - Hong,Hansol, AU - Lee,Ki Hwan, AU - Latip,Jalifah, AU - Seo,Sung-Yum, Y1 - 2020/05/11/ PY - 2020/02/04/received PY - 2020/04/08/revised PY - 2020/04/30/accepted PY - 2020/5/19/pubmed PY - 2020/5/19/medline PY - 2020/5/19/entrez KW - 4H-chromene-3-carboxylate KW - Elastase Inhibitor KW - Lipinski’s rule KW - Molecular docking KW - Multicomponent synthesis SP - 103906 EP - 103906 JF - Bioorganic chemistry JO - Bioorg. Chem. VL - 100 N2 - A new series of 4H-chromene-3-carboxylate derivatives were synthesized using multicomponent reaction of salicylaldehyde, ethyl acetoacetate and dimedone in ethanol with K3PO4 as a catalyst at 80 °C. The structures of all newly synthesized compounds were confirmed by spectral techniques viz. IR, 1H NMR, 13C NMR, and LCMS analysis. The newly synthesized compounds 4a to 4j were screened against elastase enzyme. Interestingly, all these compounds found to be potent elastase inhibitors with much lower IC50 value. The compound 4b was found to be most potent elastase inhibitor (IC50 = 0.41 ± 0.01 µM) amongst the synthesized series against standard Oleanolic Acid (IC50 value = 13.45 ± 0.0 µM). The Kinetics mechanism for compound 4b was analyzed by Lineweaver-Burk plots which revealed that compound inhibited elastase competitively by forming an enzyme-inhibitor complex. Along with this, all the synthesized compounds (4a - 4j) exhibits excellent DPPH free radical scavenging ability. The inhibition constant Ki for compound 4b was found to be 0.6 µM. The computational study was comprehensible with the experimental results with good docking energy values (Kcal/mol). Therefore, these molecules can be considered as promising medicinal scaffolds for the treatment of skin-related maladies. SN - 1090-2120 UR - https://www.unboundmedicine.com/medline/citation/32422387/Synthesis_and_characterization_of_new_4H_chromene_3_carboxylates_ensuring_potent_elastase_inhibition_activity_along_with_their_molecular_docking_and_chemoinformatics_properties_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0045-2068(20)30271-6 DB - PRIME DP - Unbound Medicine ER -
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