24730-33-4

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 5241-56-5 benzyl [(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]carbamate 
• 5241-58-7 L-Phenylalanine amide 

Downstream Products

• 86061-07-6 Fmoc-Asp(t-Bu)-Phe-NH₂ 
• 118906-07-3 Z-Glu(NPr₂)-Phe-NH₂ 
• 109736-30-3 [(R)-3-((S)-1-Carbamoyl-2-phenyl-ethylcarbamoyl)-1-dipropylcarbamoyl-propyl]-carbamic acid benzyl ester 
• 88121-96-4 Boc-Asp(Phe-NH₂)-OBzl 
• 5241-58-7 L-Phenylalanine amide 
• 109736-29-0 (R)-2-Benzoylamino-pentanedioic acid 5-[((S)-1-carbamoyl-2-phenyl-ethyl)-amide] 1-dipropylamide 
• 120452-38-2 (R)-2-[(Pyridine-4-carbonyl)-amino]-pentanedioic acid 5-[((S)-1-carbamoyl-2-phenyl-ethyl)-amide] 1-dipropylamide 
• 120452-37-1 (R)-2-(4-Chloro-benzoylamino)-pentanedioic acid 5-[((S)-1-carbamoyl-2-phenyl-ethyl)-amide] 1-dipropylamide 
• 120452-35-9 (R)-2-Amino-pentanedioic acid 5-[((S)-1-carbamoyl-2-phenyl-ethyl)-amide] 1-dipropylamide; hydrochloride 

Relevant academic research and scientific papers

Optimization and Structure-Activity Relationships of Phosphinic Pseudotripeptide Inhibitors of Aminopeptidases That Generate Antigenic Peptides

The oxytocinase subfamily of M1 aminopeptidases, consisting of ER aminopeptidase 1 (ERAP1), ER aminopeptidase 2 (ERAP2), and insulin-regulated aminopeptidase (IRAP), plays critical roles in the generation of antigenic peptides and indirectly regulates human adaptive immune responses. We have previously demonstrated that phosphinic pseudotripeptides can constitute potent inhibitors of this group of enzymes. In this study, we used synthetic methodologies able to furnish a series of stereochemically defined phosphinic pseudotripeptides and demonstrate that side chains at P1′ and P2′ positions are critical determinants in driving potency and selectivity. We identified low nanomolar inhibitors of ERAP2 and IRAP that display selectivity of more than 2 and 3 orders of magnitude, respectively. Cellular analysis demonstrated that one of the compounds that is a selective IRAP inhibitor can reduce IRAP-dependent but not ERAP1-dependent cross-presentation by dendritic cells with nanomolar efficacy. Our results encourage further preclinical development of phosphinic pseudotripeptides as regulators of adaptive immune responses.

Synthesis of Amides of Dipeptides and Kinetics of Papain-catalysed Hydrolysis of These Amides

The N-benzyloxycarbonylated amides of the dipeptides L-alanyl-L-phenylalanine, L-leucylleucine, L-leucyl-L-phenylalanine, L-phenylalanyl-L-alanine and L-phenylalanyl-L-leucine have been synthesised and the kinetic parameters for the papain-catalysed hydrolysis of these substrates and their ester analogs have been determined at pH 8 and 9.All the amide substrates are hydrolysed at the amide linkage except N-benzyloxycarbonyl-L-alanyl-L-phenylalanine amide which hydrolyses to the extent of 45percent at the amide linkage and 55percent at the peptide linkage.For amide hydrolysis acetylation and deacetylation rate constants are approximately equal.

α-AMINOACYL CONTAINING NEW PEPTIDES WITH GASTRIN EFFECTS AND A PROCESS FOR THE PREPARATION THEREOF

Peptides of the formula: wherein A is tert.-butoxycarbonyl-aminooxy-acyl, benzyloxycarbonyl-aminooxy-acyl, (aminooxy)-acyl, or E-aminooxy-acyl, wherein E is benzoyl or straight-chain or branched C1-5 aliphatic acyl, B is methionyl, leucyl, norleucyl, norvalyl or 2-amino-decanoyl, and Y is hydrogen or carboxymethoxy, and pharmaceutically acceptable acid-addition salts or complexes thereof have gastric-acid secretion increasing effects.