Silver-Induced Conformational Changes of Polypeptides
Polypeptides are polymers of amino acids linked by peptide bonds with various levels of organization. The alternative structures of the same polypeptide are referred to as different conformations, and transitions between them are called conformational changes. Silver binding to polypeptides is known to induce conformational changes, which are different from those produced by other heavy metals, such as copper, mercury, nickel, etc. The toxicity degree of silver ions seems to be modulated by their ability to change peptide and protein conformations. Glycine-rich polypeptides undergo severe conformational changes depending on the environmental conditions and especially the presence of silver ions. Contrary to other metal ions, such as copper, iron, nickel, or mercury ones, silver binding may reduce β-sheet or β-turn conformations, with the corresponding increase in the α-helical ones.
- Branden C, Tooze J (1999) Introduction to protein structure, 2nd edn. Garland Publishing, New YorkGoogle Scholar