Copper(II) complexation by fragment of central part of FBP28 protein from Mus musculus.

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 Cu2+ 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 Cu2+ ions with D17 is an entropy-driven process. Cu2+ 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.