New insights into the zinc-α2-glycoprotein (ZAG) scaffold and its metal ions binding abilities using spectroscopic techniques

In this study, fluorescence emission spectroscopy and mass spectrometry (MALDI-TOF) were employed to define the putative interaction sites and their accessibility for the biologically important metals of Irving William Series.Key findingsSeveral hotspot residues in the ZAG scaffold involved in these interactions were mapped and their binding affinity score for each metal has been determined. Their binding abilities of these sites and aggregation propensities of ZAG were monitored by fluorescence emission spectroscopy.SignificanceThe prediction of such binding affinity with metals on the active sites and its impact on the conformational states to accelerate aggregation was discussed as an important finding that may be involved in several other biochemical processes such as lipid binding, β-adrenergic receptors, cancer cachexia and association with plasma cholesterol and obesity.
Source: Life Sciences - Category: Biology Source Type: research