Novel amino acid Schiff base Zn(II) complexes as new therapeutic approaches in diabetes and Alzheimer's disease: Synthesis, characterization, biological evaluation, and molecular docking studies

ŞENOCAK A., Tas N. A., Taslimi P., TÜZÜN B., AYDIN A., KARADAĞ A.

JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, cilt.36, sa.3, 2022 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 36 Sayı: 3
  • Basım Tarihi: 2022
  • Doi Numarası: 10.1002/jbt.22969
  • Dergi Adı: JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Applied Science & Technology Source, BIOSIS, Biotechnology Research Abstracts, Chemical Abstracts Core, EMBASE, Environment Index, Food Science & Technology Abstracts, MEDLINE
  • Anahtar Kelimeler: amino acid Schiff base, enzyme inhibition, molecular docking, Zn(II) complexes, BORON COMPLEXES, INHIBITORS
  • Sivas Cumhuriyet Üniversitesi Adresli: Evet

Özet

Schiff bases are compounds that have gained importance in the paint industry due to their colorful nature and in the field of chemistry and biochemistry due to their biological activities. Various biological applications of Schiff bases, such as antitumor, antifungal, antibacterial, antioxidant, antituberculosis, and anthelmintic, have been widely studied. Within the scope of the study, 5-bromo-2-hydroxybenzaldehyde and amino acid methyl esters (isoleucine, phenylalanine, and methionine) and amino acid Schiff bases were synthesized first. The synthesis of the new Zn(II) complexes of these Schiff bases was carried out by the reaction of synthesized Schiff bases and Zn(OAc)(2)center dot 2H(2)O. The structures of the synthesized complexes were elucidated using elemental analysis, Fourier transform infrared, nuclear magnetic resonance, UV-visible, and thermal analysis spectroscopy techniques. These synthesized salts were found to be effective inhibitor compounds for the alpha-glycosidase, and acetylcholinesterase enzyme with Ki values in the range of 30.50 +/- 3.82-38.17 +/- 6.26 mu M for alpha-glycosidase, 3.68 +/- 0.54-10.27 +/- 1.68 mu M for butyrylcholinesterase, and 6.26 +/- 0.83-15.73 +/- 4.73 mu M for acetylcholinesterase, respectively.