51537-64-5

Upstream product

• 63-91-2 L-phenylalanine 
• 24424-99-5 di-tert-butyl dicarbonate 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 2393-23-9 4-methoxy-benzylamine 

Downstream Products

• 1447815-67-9 L-isoseryl-L-phenylglycyl-4-methoxybenzylamine 
• 197727-97-2 (S)-2-amino-N-(4-methoxybenzyl)-3-phenylpropanamide 
• 808149-73-7 (S)-4-Benzyl-3-[(2S,4R)-4-benzyl-5-((3aS,8aR)-2,2-dimethyl-8,8a-dihydro-3aH-indeno[1,2-d]oxazol-3-yl)-2-hydroxy-5-oxo-pentyl]-1-(4-methoxy-benzyl)-imidazolidin-2-one 
• 194599-55-8 (2R,4S)-2-Benzyl-5-((S)-5-benzyl-2-oxo-imidazolidin-1-yl)-4-hydroxy-pentanoic acid ((1S,2R)-2-hydroxy-indan-1-yl)-amide 
• 808149-68-0 (S)-4-Benzyl-1-(4-methoxy-benzyl)-imidazolidin-2-one 
• 808149-71-5 (S)-4-Benzyl-1-pyridin-4-ylmethyl-imidazolidin-2-one 
• 808149-70-4 (S)-4-Benzyl-1-pyridin-2-ylmethyl-imidazolidin-2-one 
• 808149-69-1 (S)-4-Benzyl-1-pyridin-3-ylmethyl-imidazolidin-2-one 

Relevant academic research and scientific papers

Urea-containing peptide boronic acids as potent proteasome inhibitors

A novel class of urea-containing peptide boronic acids as proteasome inhibitors was designed by introducing a urea scaffold to replace an amido bond. Compounds were synthesized and their antitumor activities were evaluated. After two rounds of optimizatio

UREA PEPTOID BORIC ACID COMPOUND, PHARMACEUTICAL COMPOSITION THEREOF, PREPARATION METHOD THEREFOR, AND USES THEREOF

The present invention provides a urea peptidomimetic boronic compound and pharmaceutical compositions thereof, their preparative methods and uses. The compounds are represented by the following formula (I).

Design, synthesis and biological evaluation of novel L-isoserine tripeptide derivatives as aminopeptidase N inhibitors

Aminopeptidase N (APN/CD13) is one of the essential proteins for tumour invasion, angiogenesis and metastasis as it is over-expressed on the surface of different tumour cells. Based on our previous work that L-isoserine dipeptide derivatives were potent APN inhibitors, we designed and synthesized L-isoserine tripeptide derivatives as APN inhibitors. Among these compounds, one compound 16l (IC50=2.51±0.2 M) showed similar inhibitory effect compared with control compound Bestatin (IC50=6.25±0.4 M) and it could be used as novel lead compound for the APN inhibitors development as anticancer agents in the future.

Copper dipicolinates as peptidomimetic ligands for the Src SH2 domain

The introduction of copper chelates into peptide mimetics creates the Src SH2 binding ligands and paramagnetic complexes suitable for EPR studies of peptide protein interactions. The dipicolinic acid was attached to SH2 domain targeting fragments by two different linkers.

Potent inhibitors of the HIV-1 protease incorporating cyclic urea P1-P2 scaffold

We have developed an efficient synthetic approach to analogues of potent HIV-protease inhibitor (PI) 4. Key chemistry includes TFA-mediated deprotection of MOB-protected 16 to precursor 17. Alkylation of 17 enabled the synthesis of many PIs, as exemplified here by 13, 19-21, in excellent yields and purity, and thus overcoming bottlenecks of our prior synthetic approach to these PIs. These results allowed to rapidly evaluate the SAR in P1-P2 cyclic urea-based HIV-1 PIs as well as provided a strong rationale towards P1-P2 pyrrolidone scaffold-based PIs, ultimately leading to subnanomolar PIs (follow-up communication). We have developed synthetic approaches to novel analogues of 2-imidazolidinone scaffold 2, which was found to be an effective P1-P2 mimetic in HIV-1 protease inhibitor 4. This enabled a rapid synthesis of analogues of 4 and subsequently allowed us to evaluate and rationalize the SAR. Accordingly, trans relationship of P1 and P2 substituents in the P1-P2 mimetic, as found in a related 2-pyrrolidone-based scaffold 1, was found necessary for high potency against HIV-1 protease. Results of this study provided further rationale towards subsequent optimization of 2-pyrrolidone-based lead 3, which led us to potent and drug-like HIV-1 protease inhibitors described in a follow-on report (Bioorg. Med. Chem. Lett. 2004, 14, in press. doi:10.1016/j.bmcl.2004.08.039).