Koseler, AylinZeytunluoğlu, AliZorlu, Yunus2023-02-072023-02-072018-09-28İnci, D. vd. (2019). ''Interaction of a new copper(II) complex by bovine serum albumin and dipeptidyl peptidase-IV''. Journal of Molecular Structure, 1177, 317-322.0022-28601872-8014https://doi.org/10.1016/j.molstruc.2018.09.086https://www.sciencedirect.com/science/article/pii/S0022286018311682http://hdl.handle.net/11452/30883Dipeptidyl 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.eninfo:eu-repo/semantics/closedAccessChemistryCu(II) complexesPyrazino[2, 3-f] [1,10]phenanthrolinePhenylalanineBovine serum albumine (BSA)Dipeptidyl peptidase-IV (DPP-IV)Crystal-structureDNA interactionsTernaryL-tyrosineAmino-acidsDNA/BSACU(II)Body fluidsChromophoresFluorescence spectroscopyFourier transform infrared spectroscopyMammalsSingle crystalsSurface plasmon resonanceBovine serum albumineCu complexesDipeptidyl peptidase ivPhenanthrolinesPhenylalanineCopper compoundsArticle0004503776000382-s2.0-850545895893173221177Chemistry, physicalComplex; Viscometry; Schiff Bases