Probing the Role of Cu(II) Ions on Protein Aggregation Using Two Model Proteins
Reshmi John, Jissy Mathew, Anu Mathew, Charuvila T. Aravindakumar, Usha K. Aravind
Abstract
, respectively. Further nanoscale morphological changes of BSA mediated by oligomers to fibril and HSA to amorphous aggregate formation were studied using atomic force microscopy. This aggregation process correlates with the Stern-Volmer plots in the absence of discernible lag phase. Raman spectroscopy results obtained are in good agreement with the increase in antiparallel β-sheet structures formed during the aggregation of BSA in the presence of Cu(II) ions. However, an increase in α-helical fractions is observed for the amorphous aggregate formed from HSA.
Topics & Concepts
IonBiophysicsChemistryProtein aggregationBiochemistryBiologyOrganic chemistryProtein Interaction Studies and Fluorescence AnalysisProtein Structure and DynamicsEnzyme Structure and Function