119706-13-7Relevant academic research and scientific papers
Unprecedented chain-length-dependent conformational conversion between 11/9 and 18/16 helix in α/β-hybrid peptides
Legrand, Baptiste,Andr, Christophe,Moulat, Laure,Wenger, Emmanuel,Didierjean, Claude,Aubert, Emmanuel,Averlant-Petit, Marie Christine,Martinez, Jean,Calmes, Monique,Amblard, Muriel
, p. 13131 - 13135 (2014)
α,β-Hybrid oligomers of varying lengths with alternating proteogenic a-amino acid and the rigid β2,3,3-trisubstituted bicyclic amino acid ABOC residues were studied using both X-ray crystal and NMR solution structures. While only an 11/9 helix
12/14/14-Helix Formation in 2:1 α/β-Hybrid Peptides Containing Bicyclo[2.2.2]octane Ring Constraints
Legrand, Baptiste,André, Christophe,Moulat, Laure,Didierjean, Claude,Hermet, Patrick,Bantignies, Jean-Louis,Martinez, Jean,Amblard, Muriel,Calmès, Monique
, p. 11986 - 11990 (2016)
The highly constrained β-amino acid ABOC induces different types of helices in β urea and 1:1 α/β amide oligomers. The latter can adopt 11/9- and 18/16-helical folds depending on the chain length in solution. Short peptides alternating proteinogenic α-ami
N-BENZHYDRYL-GLYCOLAMIDE ESTERS (OBg ESTERS) AS CARBOXYL PROTECTING GROUPS IN PEPTIDE SYNTHESIS
Amblard, Muriel,Rodriguez, Marc,Martinez, Jean
, p. 5101 - 5108 (2007/10/02)
N-benzhydryl-glycolamide esters (OBg esters) of various N-protected amino acids have been synthesized.In order to demonstrate their usefulness in peptide chemistry, the syntheses of For-Met-Leu-Phe-OH (chemiotactic peptide) and Pro-Leu-Gly-NH2 (MIF) have been carried out.OBg esters are compatible with commonly used protecting groups and are cleanly and selectively removed in mild alkaline conditions without any side reaction, except for β-benzyl aspartyl containing sequences.
