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http://hdl.handle.net/11452/30883
Başlık: | Interaction of a new copper(II) complex by bovine serum albumin and dipeptidyl peptidase-IV |
Yazarlar: | 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 |
Anahtar kelimeler: | 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 |
Yayın Tarihi: | 28-Eyl-2018 |
Yayıncı: | Elsevier |
Atıf: | 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. |
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. |
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 |
Koleksiyonlarda Görünür: | Scopus Web of Science |
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