Please use this identifier to cite or link to this item: http://hdl.handle.net/11452/30883
Title: Interaction of a new copper(II) complex by bovine serum albumin and dipeptidyl peptidase-IV
Authors: Koseler, Aylin
Zeytunluoğlu, Ali
Zorlu, Yunus
Bursa Uludağ Üniversitesi/Fen-Edebiyat Fakültesi/Kimya Bölümü.
0000-0002-0483-9642
Aydın, Rahmiye
İnci, Duygu
AAH-8936-2021
G-2201-2019
55082306300
56261495600
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
Issue Date: 28-Sep-2018
Publisher: Elsevier
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.
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.
URI: https://doi.org/10.1016/j.molstruc.2018.09.086
https://www.sciencedirect.com/science/article/pii/S0022286018311682
http://hdl.handle.net/11452/30883
ISSN: 0022-2860
1872-8014
Appears in Collections:Scopus
Web of Science

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