Encyclopedia of Metalloproteins

2013 Edition
| Editors: Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov

Silver-Induced Conformational Changes of Polypeptides

  • Gabi DrochioiuEmail author
Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_576



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.

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  1. Arrondo JL, Goni FM (1999) Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog Biophys Mol Bio 72:367–405CrossRefGoogle Scholar
  2. Branden C, Tooze J (1999) Introduction to protein structure, 2nd edn. Garland Publishing, New YorkGoogle Scholar
  3. Despax B, Saulou C, Raynaud P, Datas L, Mercier-Bonin M (2011) Transmission electron microscopy for elucidating the impact of silver-based treatments (ionic silver versus nanosilver-containing coating) on the model yeast Saccharomyces cerevisiae. Nanotechnology 22:175101CrossRefPubMedGoogle Scholar
  4. Drochioiu G, Manea M, Dragusanu M, Murariu M, Dragan ES, Petre BA, Mezo G, Przybylski M (2009) Interaction of β-amyloid(1-40) peptide with pairs of metal ions: an electrospray ion trap mass spectrometric model study. Biophys Chem 144:9–20CrossRefPubMedGoogle Scholar
  5. Havarinasab S, Pollard KM, Hultman P (2009) Gold- and silver-induced murine autoimmunity – requirement for cytokines and CD28 in murine heavy metal-induced autoimmunity. Clin Exp Immunol 155:567–576CrossRefPubMedGoogle Scholar
  6. Hultman P, Johansson U, Turley SJ, Lindh U, Eneström S, Pollard KM (1994) Adverse immunological effects and autoimmunity induced by dental amalgam and alloy in mice. FASEB J 8:1183–1190PubMedGoogle Scholar
  7. Liu X-G, Zhao J-J, Wu Q-Y (2005) Oxidative stress and metal ions effects on the cores of phycobilisomes in Synechocystis sp. PCC 6803. FEBS Lett 579:4571–4576CrossRefPubMedGoogle Scholar
  8. Murariu M, Dragan ES, Adochitei A, Zbancioc G, Drochioiu G (2011) Silver binding to peptides: a CD study. J Pept Sci 17:512–519CrossRefPubMedGoogle Scholar
  9. Pauling L, Corey RB, Branson HR (1951) The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain. Proc Natl Acad Sci USA 37:205–211CrossRefPubMedGoogle Scholar
  10. Tabarin T, Kulesza A, Antoine R, Mitrić R, Broyer M, Dugourd P, Bonačić-Koutecký V (2008) Absorption enhancement and conformational control of peptides by small silver clusters. Phys Rev Lett 101:213001CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Alexandru Ioan Cuza University of IasiIasiRomania