Faculty of Chemistry, University of Gdansk, ul. Wita Stwosza 63, 80-308 Gdansk, Poland.
Faculty of Chemistry, University of Gdansk, ul. Wita Stwosza 63, 80-308 Gdansk, Poland.
Biophys Chem. 2018 Oct;241:55-60. doi: 10.1016/j.bpc.2018.08.002. Epub 2018 Aug 7.
Steady-state and time-resolved fluorescence spectroscopy, UV spectrophotometry and isothermal titration calorimetry techniques were used to study the coordinating properties of the 17aa peptide fragment (D17) derived from the central part of the mouse formin binding protein (FBP28 with the PDB code: 1E0L) towards Cu ions. All the measurements were run in the 2-(N-morpholino)ethanesulfonic acid buffer (20 mM, pH 6.0). Under experimental conditions the formation of the 1:1 complex of Cu ions with D17 is an entropy-driven process. Cu ions cause the static fluorescence quenching of the peptide studied through the formation of a non-fluorescent complex. Furthermore, the thermal stability of D17 was discussed based on the results obtained from differential scanning fluorimetry (nanoDSF) data.
采用稳态和时间分辨荧光光谱、紫外分光光度法和等温热滴定法研究了来自小鼠formin 结合蛋白（FBP28，PDB 码：1E0L）中心部分的 17aa 肽片段（D17）与 Cu 离子的配位性质。所有测量均在 2-（N-吗啉基）乙磺酸缓冲液（20 mM，pH 6.0）中进行。在实验条件下，Cu 离子与 D17 形成 1:1 配合物是熵驱动的过程。Cu 离子通过形成非荧光配合物导致研究肽的静态荧光猝灭。此外，还根据差示扫描荧光法（nanoDSF）数据得到的结果讨论了 D17 的热稳定性。
