Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores.

ABSTRACT: Copper(II) is an essential metal in biological systems, conferring unique chemical properties to the biomolecules with which it interacts. It has been reported to directly bind to a variety of peptides and play both necessary and pathological roles ranging from mediating structure to electron transfer properties to imparting catalytic function. Quantifying the binding affinity and thermodynamics of these Cu(II)-peptide complexes in vitro provides insight into the thermodynamic driving force of binding, potential competitions between different metal ions for the peptide or between different peptides for Cu(II), and the prevalence of the Cu(II)-peptide complex in vivo. However, quantifying the binding thermodynamics can be challenging due to a myriad of factors, including accounting for all

SUBMITTER: Choi S 

PROVIDER: S-EPMC10405695 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature