Structural elucidation, molecular docking, α-amylase and α-glucosidase inhibition studies of 5-amino-nicotinic acid derivatives

Muhammad Nawaz, Muhammad Taha, Faiza Qureshi, Nisar Ullah, Manikandan Selvaraj, Sumaira Shahzad, Sridevi Chigurupati, Abdul Waheed, Fadiah Ammar Almutairi

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In this study, 5-amino-nicotinic acid derivatives (1-13) have been designed and synthesized to evaluate their inhibitory potential against α-amylase and α-glucosidase enzymes. The synthesized compounds (1-13) exhibited promising α-amylase and α-glucosidase activities. IC50 values for α-amylase activity ranged between 12.17 ± 0.14 to 37.33 ± 0.02 μg/mL ± SEM while for α-glucosidase activity the IC50 values were ranged between 12.01 ± 0.09 to 38.01 ± 0.12 μg/mL ± SEM. In particular, compounds 2 and 4-8 demonstrated significant inhibitory activities against α-amylase and α-glucosidase and the inhibitory potential of these compounds was comparable to the standard acarbose (10.98 ± 0.03 and 10.79 ± 0.17 μg/mL ± SEM, respectively). In addition, the impact of substituent on the inhibitory potential of these compounds was assessed to establish structure activity relationships. Studies in molecular simulations were conducted to better comprehend the binding properties of the compounds. All the synthesized compounds were extensively characterized with modern spectroscopic methods including 1H-NMR, 13C-NMR, FTIR, HR-MS and elemental analysis.[Figure not available: see fulltext.]

Original languageEnglish
Article number43
Number of pages11
JournalBMC Chemistry
Issue number1
Publication statusPublished - 14 Jul 2020


  • 5-Amino-nicotinic acid
  • FTIR
  • HR-MS
  • Molecular docking
  • NMR
  • Spectral studies
  • α-Amylase activity
  • α-Glucosidase activity

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