283611-32-5Relevant academic research and scientific papers
Investigation of the PDZ domain ligand binding site using chemically modified peptides
Novak, Kathleen A.P,Fujii, Naoaki,Guy
, p. 2471 - 2474 (2002)
Several chemically modified analogues to a tightly binding ligand for the second PDZ domain of MAGI-3 were synthesized and evaluated for their ability to compete with native peptide ligands. N-methyl scanning of the ligand backbone amides revealed the energetically important hydrogen bonds between the ligand backbone and the PDZ domain. Analogues to the ligand's conserved threonine/serine(-2) residue, involved in a side chain to side chain hydrogen bond with a conserved histidine in the PDZ domain, revealed that the interaction is highly sensitive to the steric structure around the hydroxyl group of this residue. Analogues of the ligand carboxy terminus revealed that the full hydrogen bond network of the GLGF loop is important in ligand binding.
N-monoalkylation of α-amino acid esters under solid-liquid PTC conditions
Albanese, Domenico,Landini, Dario,Lupi, Vittoria,Penso, Michele
, p. 1443 - 1449 (2007/10/03)
N-(2-Nitrophenylsulfonyl)- (o-NBS-AA-OMe, 4) and N-(4- Nitrophenylsulfonyl)-α-amino acid methyl esters (p-NBSAA-OMe, 5) were N- alkylated with a variety of alkyl halides 6 under solid-liquid phase-transfer catalysis (SL-PTC) conditions, affording the alkylated products o-NBS-N-R2- AA-OMe 7 and p-NBS-N-R2-AA-OMe 8 in excellent yields without any detectable racemization.
