126706-63-6

Upstream product

• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 3392-10-7 tert-butoxycarbonyl-L-proline N-hydroxysuccinimide ester 
• 2462-32-0 L-phenylalanine benzyl ester hydrochloride 
• 74257-60-6 (S)-tert-butyl 2-((S)-1-(benzyloxy)-1-oxo-3-phenylpropan-2-ylcarbamoyl)pyrrolidine-1-carboxylate 

Downstream Products

• 357429-23-3 N-{N-[(2S)-4-oxoazetidine-2-carbonyl]-L-(benzyl)histidyl}-L-prolyl-L-phenylalanine benzyl ester 
• 357429-22-2 N-{N-[(2S)-1-(tert-butyldimethylsilyl)-4-oxoazetidine-2-carbonyl]-L-(benzyl)histidyl}-L-prolyl-L-phenylalanine benzyl ester 
• 5654-85-3 (3S,8aS)-3-benzyloctahydropyrrolo[1,2-a]pyrazine-1,4-dione 
• 78746-24-4 N-Boc-L-(benzyl)histidyl-L-prolyl-L-phenylalanine benzyl ester 

Relevant academic research and scientific papers

Copper(II) Complexes with Some Tetrapeptides containing the 'Break-point' Prolyl Residue in the Third Position

The tetrapeptides Phe-Gly-Pro-Phe, Phe-Gly-Pro-Tyr, and Tyr-Gly-Pro-Phe have been synthesised and their complexes with H+ and Cu2+ studied by potentiometry and spectroscopy (u.v., visible, c.d., and e.s.r.) at 25 deg C and I=0.10 mol

Molecular capture and conformational change of diketopiperazines containing proline residues by epigallocatechin-3-O-gallate in water

The addition of an aqueous solution of diketopiperazine cyclo(Pro-Xxx) (Xxx: amino acid residue) to an aqueous solution of (?)-epigallocatechin-3-O-gallate (EGCg) led to precipitation of the complex of EGCg and cyclo(Pro-Xxx). The molecular capture abilities of cyclo(Pro-Xxx) using EGCg were evaluated by the ratio of the amount of cyclo(Pro-Xxx) included in the precipitates of the complex with EGCg to that of the total cyclo(Pro-Xxx) used. Stronger hydrophobicity of the side chain of the amino acid residue of cyclo(Pro-Xxx) led to a higher molecular capture ability. Furthermore, the molecular capture ability decreased when the side chain of the amino acid residue had a hydrophilic hydroxyl group. When diketopiperazine cyclo(Pro-Xxx), excluding cyclo(D-Pro-L-Ala), was taken into the hydrophobic space formed by the three aromatic A, B, and B′ rings of EGCg, and formed a complex, their conformation was maintained in the hydrophobic space. Based on nuclear Overhauser effect (NOE) measurement, the 3-position methyl group of cyclo(D-Pro-L-Ala) in D2O was axial, whereas that of cyclo(L-Pro-L-Ala) was equatorial. When cyclo(D-Pro-L-Ala) was taken into the hydrophobic space of EGCg and formed a 2:2 complex, its 3-position methyl group changed from the axial position to the equatorial position due to steric hindrance by EGCg.

β-lactam derivatives as enzyme inhibitors: Carboxy peptidyl derivatives of (S)-4-Oxoazetidine-2-carboxylate as peptidomimetics

4-Oxoazetidine-2-carboxylic acid, protected at the nitrogen by silyl groups, was coupled with amino acid and oligopeptide esters. Desilylation and deprotection of the amino acid residues yielded the free β-lactam peptides. Structure and properties were elucidated by spectroscopic methods and discussed. Some selected compounds Were tested as fibrinogen inhibitors and for thrombocyte aggregation. None of the compounds showed any activity up to a concentration of 10-5 Mol/1. Some other compounds exhibited a weak inhibitory activity against elastase (PPE).