Design, synthesis and structural investigations of a beta-peptide forming a 3(14)-helix stabilized by electrostatic interactions

Two different strategies have been employed for the synthesis of Fmoc-protected beta(3)-homoarginine; the Arndt-Eistert homologation of alpha-arginine and the guanidinylation of beta(3)-homoornithine. Solid-phase beta-peptide synthesis was used for the preparation of beta-heptapeptide 1, which was d...

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Published inChemistry : a European journal Vol. 10; no. 7; pp. 1607 - 1615
Main Authors Rueping, M, Mahajan, YR, Jaun, B, Seebach, D
Format Journal Article
LanguageEnglish
Published WEINHEIM Wiley 02.04.2004
Subjects
Chemistry
Chemistry, Multidisciplinary
Physical Sciences
Science & Technology
HELICAL SECONDARY STRUCTURE
SOLID-PHASE SYNTHESIS
ACIDS
helical structures
CD SPECTRA
CELLULAR UPTAKE
SIDE-CHAINS
SPECTROSCOPIC EVIDENCE
NMR-SOLUTION STRUCTURE
beta-peptides
ARGININE
salt bridges
NMR spectroscopy
electrostatic interactions
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Summary:Two different strategies have been employed for the synthesis of Fmoc-protected beta(3)-homoarginine; the Arndt-Eistert homologation of alpha-arginine and the guanidinylation of beta(3)-homoornithine. Solid-phase beta-peptide synthesis was used for the preparation of beta-heptapeptide 1, which was de- signed to form a helix stabilized by electrostatic interactions through positively (beta(3)hArg) and negatively charged (beta(3)hGlu) amino acid residues. CD measurements and corresponding NMR investigations in MeOH and aqueous solutions do indeed show that the beta-peptidic 3(14)-helix can be stabilized by salt-bridge formation.
ISSN:0947-6539
1521-3765
DOI:10.1002/chem.200305571