Inducing α-Helicity in Peptides by Silver Coordination to Cysteine
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Inducing α-Helicity in Peptides by Silver Coordination to Cysteine. / Fischer, Niklas; Tóth, Annamária; Jancsó, Attila; Thulstrup, Peter; Diness, Frederik.
In: Chemistry - A European Journal, Vol. 30, No. 31, e202304064, 2024.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Inducing α-Helicity in Peptides by Silver Coordination to Cysteine
AU - Fischer, Niklas
AU - Tóth, Annamária
AU - Jancsó, Attila
AU - Thulstrup, Peter
AU - Diness, Frederik
N1 - Funding Information: The authors are grateful for financial support to this project from the Novo Nordisk Foundation (NNF18OC0034734). The authors acknowledge Dr. Ria\u2005K. Balogh for technical assistance with preparation and quantification of metal ion solutions. Publisher Copyright: © 2024 The Authors. Chemistry - A European Journal published by Wiley-VCH GmbH.
PY - 2024
Y1 - 2024
N2 - 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.
AB - 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.
KW - cysteine
KW - oligomerization
KW - peptide
KW - silver
KW - α-helix
U2 - 10.1002/chem.202304064
DO - 10.1002/chem.202304064
M3 - Journal article
C2 - 38456607
AN - SCOPUS:85192804996
VL - 30
JO - Chemistry: A European Journal
JF - Chemistry: A European Journal
SN - 0947-6539
IS - 31
M1 - e202304064
ER -
ID: 395085764