Design, synthesis and structural investigations of a beta-peptide forming a 314-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 designed 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.
Rueping
Magnus
M
Laboratorium für Organische Chemie, der Eidgenössischen Technischen Hochschule Zürich, ETH-Hönggerberg, Wolfgang-Pauli-Strasse 10, 8093 Zürich, Switzerland.
Mahajan
Yogesh R
YR
Jaun
Bernhard
B
Seebach
Dieter
D
D001120:Arginine / Q000138:chemical synthesis / Q000737:chemistry; D002942:Circular Dichroism; D008956:Models, Chemical; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D055672:Static Electricity
D010446:Peptide Fragments; D001120:Arginine