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Silver-induced conformational changes of polypeptides: a CD study

✍ Scribed by Manuela Murariu; Ecaterina Stela Dragan; Adriana Adochitei; Gheorghita Zbancioc; Gabi Drochioiu

Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
231 KB
Volume
17
Category
Article
ISSN
1075-2617

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✦ Synopsis

Abstract

The role of silver ions in various pathologies, as well as their effect on peptide conformation and properties are less understood. Consequently, we synthesized several peptides with various residues in their sequence to investigate silver‐induced conformational changes at various pH values by Circular Dichroism spectroscopy. Uniquely, the glycine‐based, histidine‐containing peptide showed a severe change from a random coil and β‐turn conformation to large α‐helices during silver binding. When comparing the effect of silver ions on the conformation of bradykinin a similar tendency was found. Besides, silver ions reduced the amyloid‐β peptide tendency to aggregation. Our results suggest a specific and protective role for silver ions in brain pathologies, which is related to their high affinity toward physiologically and pharmacologically active peptides. Fourier transform infrared spectroscopy studies as well as the mass spectrometric ones support our conclusions. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.

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