Synthesis of new arylhydrazide bearing Schiff bases/thiazolidinone: α-Amylase, urease activities and their molecular docking studies

Rahim F 1 , Taha M 2 , Ullah H 3 , Wadood A 4 , Selvaraj M 5 , Rab A 3 Show all authors , Sajid M 6 , Shah SAA 7 , Uddin N 8 , Gollapalli M 9

Affiliations 

  • 1 Department of Chemistry, Hazara University, Mansehra 21300, Khyber Pakhtunkhwa, Pakistan. Electronic address: fazalstar@gmail.com
  • 2 Department of Clinical Pharmacy, Institute for Research and Medical Consultations (IRMC), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, Dammam 31441, Saudi Arabia. Electronic address: mtaha@iau.edu.sa
  • 3 Department of Chemistry, Hazara University, Mansehra 21300, Khyber Pakhtunkhwa, Pakistan
  • 4 Department of Biochemistry, Abdul Wali Khan University Mardan, Mardan 23200, Pakistan
  • 5 Monash University School of Chemical Engineering, Bandar Subway, 47500 Selangor Alam Campus, 42300, Malaysia
  • 6 Department of Biochemistry, Hazara University, Mansehra 21300, Khyber Pakhtunkhwa, Pakistan
  • 7 Atta-ur-Rahman Institute for Natural Products Discovery (AuRIns), Universiti Teknologi MARA Cawangan Selangor Kampus Puncak Alam, 42300 Bandar Puncak Alam, Selangor D. E., Malaysia.; Faculty of Pharmacy, Universiti Teknologi MARA Cawangan Selangor Kampus Puncak Alam, 42300 Bandar Puncak Alam, Selangor D. E., Malaysia
  • 8 Department of Chemistry, University of Karachi, Karachi 75270, Pakistan
  • 9 Department of Computer Information Systems, College of Computer Science & Information Technology (CCSIT), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, Dammam 31441, Saudi Arabia
Bioorg Chem, 2019 10;91:103112.
PMID: 31349115 DOI: 10.1016/j.bioorg.2019.103112

Abstract

Alpha-amylase and urease enzyme over expression endorses various complications like rheumatoid arthritis, urinary tract infection, colon cancer, metabolic disorder, cardiovascular risk, and chronic kidney disease. To overcome these complications, we have synthesized new arylhydrazide bearing Schiff bases/thiazolidinone analogues as α-amylase and urease inhibitors. The analogues 1a-r were evaluated for α-amylase inhibitory potential. All analogues were found active and show IC50 value ranging between 0.8 ± 0.05 and 12.50 ± 0.5 μM as compare to standard acarbose (IC50 = 1.70 ± 0.10 μM). Among the synthesized analogs, compound 1j, 1r, 1k, 1e, 1b and 1f having IC50 values 0.8 ± 0.05, 0.9 ± 0.05, 1.00 ± 0.05, 1.10 ± 0.10, 1.20 ± 0.10 and 1.30 ± 0.10 μM respectively showed an excellent inhibitory potential. Analogs 2a-o were evaluated against urease activity. All analogues were found active and show IC50 value ranging between 4.10 ± 0.02 and 38.20 ± 1.10 μM as compare to standard thiourea (IC50 = 21.40 ± 0.21 μM). Among the synthesized analogs, compound 2k, 2a, 2h, 2j, 2f, 2e, 2g, 2b and 2l having IC50 values 4.10 ± 0.02, 4.60 ± 0.02, 4.70 ± 0.03, 5.40 ± 0.02, 6.70 ± 0.05, 8.30 ± 0.3, 11.20 ± 0.04, 16.90 ± 0.8 and 19.80 ± 0.60 μM respectively showed an excellent inhibitory potential. All compounds were characterized through 1H, 13C NMR and HR-EIMS analysis. Structure activity relationship of the synthesized analogs were recognized and confirmed through molecular docking studies.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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