2537-91-9

Upstream product

• 19391-50-5 (S)-methyl 2-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)-3-(4-hydroxyphenyl)propanoate 
• 3417-91-2 L-tyrosine methyl ester HCl 
• 60-18-4 L-tyrosine 
• 1080-06-4 L-Tyr-OMe 
• 109453-49-8 (C₈H₇O₂)(NHCHCOO)(CH₂C₆H₅)(CO₂C₂H₅) 
• 41518-17-6 Z-Phe-O-COO-isoBu 
• 18689-44-6 N-Benzyloxycarbonyl-O-ethoxycarbonyl-L-tyrosin-methylester 
• 18706-82-6 N-Benzyloxycarbonyl-O-ethoxycarbonyl-L-tyrosin 
• 1161-13-3 N-Cbz-L-Phe 
• 1164-16-5 Z-L-Tyr-OH 
• 501-53-1 benzyl chloroformate 
• 63-91-2 L-phenylalanine 
• 18689-48-0 N-Benzyloxycarbonyl-L-phenylalanyl-O-ethoxycarbonyl-L-tyrosin-methylester 
• 3392-15-2 N-benzyloxycarbonyl-L-phenylalanyl-L-tyrosine ethyl ester 

Downstream Products

• 1161-13-3 N-Cbz-L-Phe 
• 60-18-4 L-tyrosine 

Relevant academic research and scientific papers

Ecological base-conditioned preparation of dipeptides using unprotected α-amino acids containing hydrophilic side chains

The coupling reactions of 3-phenylpropanoic acid and Ncarboxybenzyl á-amino acids with unprotected á-amino acids containing hydrophilic side chains such as aliphatic alcohol, aromatic alcohol, thiol, carboxylic acid, and amide afforded the corresponding amides in 6696% yield without racemization via the corresponding mixed carbonic carboxylic anhydrides under basic conditions through an ecological green synthetic method.

Synthesis, bioactivity, docking and molecular dynamics studies of furan-based peptides as 20s proteasome inhibitors

Proteasome inhibitors are promising compounds for a number of therapies, including cardiovascular and eye diseases, diabetes, and cancers. We previously reported a series of furanbased peptidic inhibitors with moderate potencies against the proteasome b5 subunit, hypothesizing that the C-terminal furyl ketone motif could form a covalent bond with the catalytic residue, threonine 1. In this context, we describe further optimizations of the furan-based peptides, and a series of dipeptidic and tripeptidic inhibitors were designed and synthesized, aiming at improved potency and better solubility. Most of the tripeptidic inhibitors demonstrated improved potency and selectivity as b5 subunit inhibitors in both enzymatic and cellular assays, and good antineoplastic activities in various tumor cell lines were also observed. However, no inhibitory effects were observed for the dipeptidic compounds, which led us to presume that a noncovalent binding mode is adopted. Docking studies and molecular dynamics simulations were carried out to verify this presumption, with results showing that the distance between the furyl ketone motif and Thr1 is slightly too long to form covalent bond.

α-N-Protected dipeptide acids: A simple and efficient synthesis via the easily accessible mixed anhydride method using free amino acids in DMSO and tetrabutylammonium hydroxide

The importance of dipeptides both in medicinal and pharmacological fields is well documented and many efforts have been made to find simple and efficient methods for their synthesis. For this reason, we have investigated the synthesis of α-N-protected dipeptide acids by reacting the easily accessible mixed anhydride of α-N-protected amino acids with free amino acids under different reaction conditions. The combination of TBA-OH and DMSO has been found to be the best to overcome the low solubility of amino acids in organic solvents. Under these experimental conditions, the homogeneous phase condensation reaction occurs rapidly and without detectable epimerization. The present method is also applicable to side-chain unprotected Tyr, Trp, Glu, and Asp but not Lys. This latter residue is able to engage two molecules of mixed anhydride giving the corresponding isotripeptide. Moreover, the applicability of this protocol for the synthesis of tri- and tetrapeptides has been tested. This approach reduces the need for protecting groups, is cost effective, scalable, and yields dipeptide acids that can be used as building blocks in the synthesis of larger peptides.

Relationship between the hydrophobicity of dipeptides and the Michaelis-Menten constant Km of their hydrolysis by carboxypeptidase-Y and carboxypeptidase-A

The enzymatic hydrolysis of dipeptides by carboxypeptidase-Y and carboxypeptidase-A was investigated. In the enzymatic hydrolysis of the dipeptides, a good linear relationship (r = 0.997 and 0.999) was found between the Michaelis-Menten constant (Km) and the hydrophobicity of the substrates evaluated from relative elution volume in reversed-phase HPLC. The correlation suggests that the hydrophobicity of the C-terminal amino acid is a major factor in governing the stability of the enzyme-substrate complex. The difference in the slope of the linear-regression lines seems to reflect the degree of relative hydrophobicity of the binding pockets in carboxypeptidase-Y and carboxypeptidase-A.

Pharmaceutical composition having an excellent absorption property

A compound represented by the formula: STR1 wherein R1 is a hydrogen atom, a fluorine atom, a nitro group, a hydroxyl group or a hydroxyl group protected by an esterifying group; X is CO or SO2 ; --Y-- is a straight bond, a lower alkylene group, a substituted or unsubstituted vinylene group, or group having the formula --CH2 --O-- or --O--CH2 --; R2 is a substituted or unsubstituted phenyl or naphthyl group, or R2 --Y--CO is N-benzyloxycarbonylphenylalanyl, N-benzyloxycarbonyl-4-fluorophenylalanyl or N-(m-methoxycinnamoyl)-phenylalanyl group; or a non-toxic salt thereof is disclosed along with pharmaceutical compositions containing these compounds and methods of using these compositions to increase the rate of absorption of medicines.