157756-00-8

Upstream product

• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 
• 107-15-3 ethylenediamine 
• 2578-84-9 N-benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester 
• 1161-13-3 N-Cbz-L-Phe 

Downstream Products

• 102036-11-3 N,N'-bis(phenylalanyl)ethane-1,2-diamine 

Relevant academic research and scientific papers

Chiral Diaminodiamide Copper(II) Complexes for the Enantioselective Recognition of Amino Acids: Synthesis of the Ligands and Formation Constants

(S,S)-N,N'-Bis(aminoacyl)ethane and (S,S)-bis(aminoacyl)propanediamines (AA-NN-2 and AA-NN-3, respectively, AA = alanine, phenylalanine, valine) were synthesized as the dihydrochlorides, and their complexes with Cu(II) studied potentiometrically.Since the

Copper(ii) complexes of macrocyclic and open-chain pseudopeptidic ligands: synthesis, characterization and interaction with dicarboxylates

Mono- and dinuclear Cu(ii) complexes were prepared with pseudopeptidic open chain and macrocyclic ligands, respectively. They were characterized by UV-vis spectroscopy, EPR, HRMS and X-ray diffraction. The Cu(ii) cation is coordinated by two amines and tw

A simple peptidomimetic that self-associates on the solid state to form a nanoporous architecture containing chiral π-channels

The crystal structure of a simple peptidomimetic compound, derived from phenylalanine, shows the formation of a nanoporous architecture containing monodimensional π-channels with the aromatic rings as the exclusive components of the chiral channel walls. The Royal Society of Chemistry 2010.

Chiral bis(amino amides) as chiral solvating agents for enantiomeric excess determination of α-hydroxy and arylpropionic acids

A family of bis(amino amides) derived from natural amino acids has been synthesized and tested for the NMR enantiodiscrimination, as chiral solvating agents, for enantiomeric excess determination of some carboxylic acids. Those bis(amino amide) receptors contain different structural modifications and the splitting of the signals of the acids, after addition of the corresponding CSAs, depends on those structural variables. The influence of aminoacid side chain and the nature of the aliphatic spacer are important parameters to obtain good chiral discriminations. The results obtained clearly show the chiral recognition abilities of these bis(amino amide) ligands and suggest their advantageous use as chiral solvating agents for carboxylic acids. The binding between bis(amino amides) and carboxylic acids has been studied by ESI-MS, NMR, DSC, and molecular modeling. The data suggest that enantiodiscrimination involves the formation of an ionic pair after proton transfer from the carboxylic substrate to the bis(amino amides).

Efficient macrocyclization of U-turn preorganized peptidomimetics: The role of intramolecular H-bond and solvophobic effects

Simple peptidomimetic molecules derived from amino acids were reacted with meta- and parabis(bromomethyl) benzene in acetonitrile to very efficiently yield macrocyclic structures. The cyclization reaction does not require high dilution techniques and seems to be insensitive to the size of the formed macrocycle. The analysis of data obtained by 1H NMR, single-crystal X-ray diffraction, fluorescence measurements, and molecular mechanics indicate that folded conformations can preorganize the system for an efficient cyclization. The role played by intramolecular hydrogen-bonding and solvophobic effects in the presence of folded conformations is analyzed.

Photochemistry of dipeptides in aqueous solution

The photochemical lability of peptides is poorly understood, largely because of the lack of product data. In the present study, product analyses have been carried out following the photolyses in aqueous solution of selected glycyl dipeptides (Gly-Gly, DL-Ala-Gly, L-Val-Gly, L-Pro-Gly, L-Phe-Gly, and Gly-L-Phe), L-prolyl-L-phenylalanine, and L-phenylalanyl-L-proline. Efficient deamination and decarboxylation of aliphatic dipeptides generate thermal precursors of simple amides in a photoinduced electron-transfer process involving the peptide bond. An analogous pathway in the photodegradation of phenylalanyl peptides suffers competition from other types of reaction.