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Design, Synthesis and Structural Investigations of a β‐Peptide Forming a 3 14 ‐Helix Stabilized by Electrostatic Interactions
Author(s) -
Rueping Magnus,
Mahajan Yogesh R.,
Jaun Bernhard,
Seebach Dieter
Publication year - 2004
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200305571
Subject(s) - helix (gastropod) , electrostatics , materials science , peptide , crystallography , nanotechnology , chemistry , biochemistry , biology , snail , ecology
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.