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Protein Science, Vol 6, Issue 7 1396-1404, Copyright © 1997 by Cold Spring Harbor Laboratory Press

ARTICLE

Design and characterization of the anion-sensitive coiled-coil peptide

M. HOSHINO, N. YUMOTO, S. YOSHIKAWA and Y. GOTO
Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560, Japan

As a model for analyzing the role of charge repulsion in proteins and its shielding by the solvent, we designed a peptide of 27 amino acid residues that formed a homodimeric coiled-coil. The interface between the coils consisted of hydrophobic Leu and Val residues, and 10 Lys residues per monomer were incorporated into the positions exposed to solvent. During the preparation of a disulfide-linked dimer in which the two peptides were linked in parallel by the two disulfide bonds located at the N and C terminals, a cyclic monomer with an intramolecular disulfide bond was also obtained. On the basis of CD and (1)H-NMR, the conformational stabilities of these isomers and several reference peptides were examined. Whereas all these peptides were unfolded in the absence of salt at pH 4.7 and 20{deg}C, the addition of NaClO(4) cooperatively stabilized the {alpha}-helical conformation. The crosslinking of the peptides by disulfide bonds significantly decreased the midpoint salt concentration of the transition. The (1)H-NMR spectra in the presence of NaClO(4) suggested that, whereas the disulfide-bonded dimer assumed a native-like conformation, the cyclic monomer assumed a molten globule-like conformation with disordered side chains. However, the cyclic monomer exhibited cooperative transitions against temperature and Gdn-HCl that were only slightly less cooperative than those of the disulfide-bonded parallel dimer. These results indicate that the charge repulsion critically destabilizes the native-like state as well as the molten globule-like state, and that the solvent-dependent charge repulsion may be useful for controlling the conformation of designed peptides.
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