Inducing α-Helicity in Peptides by Silver Coordination to Cysteine.

Chemistry

Department of Science and Environment, Roskilde University, Universitetsvej 1, 4000, Roskilde, Denmark.

Published: June 2024

Short peptide sequences consisting of two cysteine residues separated by three other amino acids display complete change from random coil to α-helical secondary structure in response to addition of Ag ions. The folded CXXXC/Ag complex involves formation of multinuclear Ag species and is stable in a wide pH range from below 3 to above 8. The complex is stable through reversed-phase HPLC separation as well as towards a physiological level of chloride ions, based on far-UV circular dichroism spectroscopy. In electrospray MS under acidic conditions a peptide dimer with four Ag ions bound was observed, and modelling based on potentiometric experiments supported this to be the dominating complex at neutral pH together with a peptide dimer with 3 Ag and one proton at lower pH. The complex was demonstrated to work as a N-terminal nucleation site for inducing α-helicity into longer peptides. This type of silver-mediated peptide assembly and folding may be of more general use for stabilizing not only peptide folding but also for controlling oligomerization even under acidic conditions.

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http://dx.doi.org/10.1002/chem.202304064DOI Listing

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