Interaction of a new copper(II) complex by bovine serum albumin and dipeptidyl peptidase-IV

Inci D., KÖSELER A., ZEYTÜNLÜOĞLU A., AYDIN R., ZORLU Y.

JOURNAL OF MOLECULAR STRUCTURE, cilt.1177, ss.317-322, 2019 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 1177
  • Basım Tarihi: 2019
  • Doi Numarası: 10.1016/j.molstruc.2018.09.086
  • Dergi Adı: JOURNAL OF MOLECULAR STRUCTURE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.317-322
  • Anahtar Kelimeler: Cu(II) complexes, pyrazino[2, 3-f] [1,10]phenanthroline, Phenylalanine, Bovine serum albumine (BSA), dipeptidyl peptidase-IV (DPP-IV), CRYSTAL-STRUCTURE, DNA INTERACTIONS, AMINO-ACIDS, L-TYROSINE, TERNARY, DNA/BSA, CU(II)
  • Bursa Uludağ Üniversitesi Adresli: Evet

Özet

Dipeptidyl peptidase-IV (DPP-IV) is one of the mammalian serine proteases participated in the pathogenesis of diseases and DPP-IV inhibitors are now widely used as antidiabetic drugs. A new water soluble ternary copper (II) complex,-[Cu(PY-Phen) (phe) (H2O)]NO3 center dot H2O-(py-phen:pyrazino[2,3f][1,10]phenanthroline, phe:phenylalanine), has been synthesized and characterized by CHN analysis, ESI-MS, FTIR and single-crystal X-ray diffraction techniques. Fluorescence spectroscopy was researched to study the interaction between the complex and bovine serum albumin (BSA) and dipeptidyl peptidase-IV (DPP-IV). Chromophore of BSA and DPP-IV enzyme is changed upon addition of the complex. Additionally, the complex was shown to have promising inhibitory activities against DPP-IV with lower IC50 value. This study may provide new insights into the development of effective agents against diabetes. (C) 2018 Elsevier B.V. All rights reserved.