Open AccessSolid-Phase Synthesis of β-Oligopeptides
Author(s) -
Gilles Guichard,
Dieter Seebàch
Publication year - 1997
Publication title -
chimia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.387
H-Index - 55
eISSN - 2673-2424
pISSN - 0009-4293
DOI - 10.2533/chimia.1997.315
Subject(s) - chemistry , yield (engineering) , peptide , peptide synthesis , chromatography , organic chemistry , stereochemistry , biochemistry , materials science , metallurgy
Fmoc-N-Protected β-amino acids of (S)-configuration bearing the side chains of Ala, Val, Leu, and Phe in the 3- and 2-position have been prepared. Manual solid-phase synthesis (ortho-chlorotrityl-chloride resin) of the β-heptapeptides H-β3-HVal-β3-HAla-β3-HLeu-β3-HPhe-β3-HVal-β3-HAla-β3-HLeu-OH and H-β2-HVal-β2-HAla-β2-HLeu-β2-HPhe-β2-HVal-β2-HAla-β2-HLeu-OH, and, for comparison, of the corresponding α-heptapeptide H-Val-Ala-Leu-Phe-Val-Ala-Leu-OH was achieved under standard conditions (HPLC/NMR identification). With H-β3-HVal-β3-HAla-β3-HLeu-β3-HPhe-β3-HVal-β3-HAla-β3-HLeu-OH, the yield and purity of the crude product are similar to those of H-Val-Ala-Leu-Phe-Val-Ala-Leu-OH, while the β2 synthesis needs to be optimized. CD measurements show that the β-peptides have helical secondary structures in MeOH, while the α-peptide does not.