Seminarium Zakładu Biofizyki

Phosphorylation modulates many protein functions, including enzymatic activity and binding to other proteins, nucleic acids, or lipid membranes. It changes the charge of the modified side chain and may therefore influence protein structure and function. Metal ions, such as copper, have an analogous impact on protein function. However, little is known about the molecular interplay between phosphorylation and metal binding.Our study aimed to determine how the phosphorylation of serine residues in the vicinity of copper-binding sites changes the metal-peptide binding affinity. We tested the impact of the distance of the modified serine to the metal-binding site and the influence of Cu(II) binding mode using various human peptides. Understanding such phenomena is relevant to diseases characterized by phosphorylation and metal ion dysregulation, such as cancer, as well as autoimmune, neurodegenerative, and cardiovascular diseases.