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- Title
Zn<sup>2+</sup>-Complexation by a β-Peptidic Helix and Hairpin Containing β<sup>3</sup>hCys and β<sup>3</sup>hHis Building Blocks: Evidence from CD Measurements. Preliminary Communication.
- Authors
Francesco Rossi; Gérald Lelais; Dieter Seebach
- Abstract
Two new β3-homohistidine- and β3-homocysteine-containing β-peptides have been prepared by solid-phase synthesis. A β-octapeptide (2) contains seven β3-amino acids and one β2-amino acid. The β2/β3 segment has been placed in the middle of this peptide, which contains β3-amino acids of alternating configuration, to induce the formation of a hairpin secondary structure. A β-decapeptide (3) has been designed to fold to a 314-helical secondary structure with neighboring His side chains in 6- and 9-positions. Circular-dichroism (CD) measurements show the capability of both peptides to bind Zn2+ ions in aqueous solution. In the case of the β-octapeptide, binding of Zn2+ causes a dramatic change of the CD spectrum, indicating a change or a stabilization of its secondary structure. Zn2+ Ions clearly stabilize the 314-helix of the β-decapeptide, in neutral and basic solution. For the construction of the two new β-peptides, we needed to have a supply of the β-amino acid derivatives Fmoc-β3hCys(Trt)-OH and Fmoc-β3hHis(Trt)-OH, the preparation of which is described herein.
- Subjects
PEPTIDES; HOMOCYSTEINE; AMINO acids
- Publication
Helvetica Chimica Acta, 2003, Vol 86, Issue 7, p2653
- ISSN
0018-019X
- Publication type
Article