Inducing α-Helicity in Peptides by Silver Coordination to Cysteine

被引:1
|
作者
Fischer, Niklas [1 ,2 ]
Toth, Annamaria [3 ]
Jancso, Attila [3 ]
Thulstrup, Peter [2 ]
Diness, Frederik [1 ,2 ]
机构
[1] Roskilde Univ, Dept Sci & Environm, Univ Vej 1, DK-4000 Roskilde, Denmark
[2] Univ Copenhagen, Dept Chem, Univ Pk 5, DK-2100 Copenhagen O, Denmark
[3] Univ Szeged, Dept Mol & Analyt Chem, Domter 7-8, H-6720 Szeged, Hungary
关键词
alpha-helix; oligomerization; silver; cysteine; peptide; DESIGNED PEPTIDE; BINDING-SITES; METAL-IONS; HELIX; PROTEIN; PENTAPEPTIDES; DISRUPTION; NUCLEATION; STABILITY; COMPLEXES;
D O I
10.1002/chem.202304064
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Short peptide sequences consisting of two cysteine residues separated by three other amino acids display complete change from random coil to alpha-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 alpha-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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页数:6
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