Interaction of a new copper(II) complex by bovine serum albumin and dipeptidyl peptidase-IV
No Thumbnail Available
Date
2018-09-28
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier
Abstract
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.
Description
Keywords
Chemistry, Cu(II) complexes, Pyrazino[2, 3-f] [1,10]phenanthroline, Phenylalanine, Bovine serum albumine (BSA), Dipeptidyl peptidase-IV (DPP-IV), Crystal-structure, DNA interactions, Ternary, L-tyrosine, Amino-acids, DNA/BSA, CU(II), Body fluids, Chromophores, Fluorescence spectroscopy, Fourier transform infrared spectroscopy, Mammals, Single crystals, Surface plasmon resonance, Bovine serum albumine, Cu complexes, Dipeptidyl peptidase iv, Phenanthrolines, Phenylalanine, Copper compounds
Citation
İnci, D. vd. (2019). ''Interaction of a new copper(II) complex by bovine serum albumin and dipeptidyl peptidase-IV''. Journal of Molecular Structure, 1177, 317-322.