Design, Synthesis and Structural Investigations of a β-Peptide Forming a 314-Helix Stabilized by Electrostatic Interactions
✍ Scribed by Magnus Rueping; Yogesh R. Mahajan; Bernhard Jaun; Dieter Seebach
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 374 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0947-6539
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✦ Synopsis
Abstract
Two different strategies have been employed for the synthesis of Fmoc‐protected β^3^‐homoarginine; the Arndt–Eistert homologation of α‐arginine and the guanidinylation of β^3^‐homoornithine. Solid‐phase β‐peptide synthesis was used for the preparation of β‐heptapeptide 1, which was designed to form a helix stabilized by electrostatic interactions through positively (β^3^hArg) and negatively charged (β^3^hGlu) amino acid residues. CD measurements and corresponding NMR investigations in MeOH and aqueous solutions do indeed show that the β‐peptidic 3~14~‐helix can be stabilized by salt‐bridge formation.