286436-68-8

Upstream product

• 291312-78-2 H-L-Asu(OBzl)-Aib-L-Phe-D-Pro-OH TFA salt 
• 1161-13-3 N-Cbz-L-Phe 
• 1247052-87-4 benzyl 6-[(3S,9S,14aR)-9-benzyl-6,6-dimethyl-1,4,7,10-tetraoxotetradecahydropyrrolo[1,2-a][1,4,7,10]tetraazacyclododecin-3-yl]-4-(ethoxycarbonothioylthio)hexanoate 
• 1247052-65-8 (-)-(3S,9S,14aR)-9-benzyl-3-(but-3-enyl)-6,6-dimethyldecahydropyrrolo[1,2-a][1,4,7,10]tetraazacyclododecine-1,4,7,10-tetraone 
• 1247052-63-6 C₃₃H₅₀N₄O₇ 
• 92136-57-7 (S)-2-tert-butoxycarbonylamino-hex-5-enoic acid methyl ester 
• 221186-92-1 Boc-L-Asu(OBzl)-Aib-L-Phe-D-Pro-OtBu 
• 221186-91-0 Z-Aib-L-Phe-D-Pro-OtBu 
• 291312-77-1 H-Aib-L-Phe-D-Pro-OtBu 
• 162757-06-4 Z-L-Phe-D-Pro-OtBu 
• 221186-79-4 (+)-(R)-tert-butyl 1-[(S)-2-amino-3-phenylpropanoyl]pyrrolidine-2-carboxylate 
• 2812-46-6 L-proline t-butyl ester 

Downstream Products

• 104849-05-0 cyclo[2-aminoisobutyryl-(S)-phenylalanyl-(R)-prolyl-(S)-2-aminosuberoyl-] 

Relevant academic research and scientific papers

Flexible synthesis and evaluation of diverse anti-apicomplexa cyclic peptides

A modular approach to synthesize anti-Apicomplexa parasite inhibitors was developed that takes advantage of a pluripotent cyclic tetrapeptide scaffold capable of adjusting appendage and skeletal diversities in only a few steps (one to three steps). The diversification processes make use of selective radical coupling reactions and involve a new example of a reductive carbon-nitrogen cleavage reaction with SmI2. The resulting bioactive cyclic peptides have revealed new insights into structural factors that govern selectivity between Apicomplexa parasites such as Toxoplasma and Plasmodium and human cells.

CYCLIC PEPTIDES WITH AN ANTI-PARASITIC ACTIVITY

The present invention relates to a method for preparing a cyclic peptide with antiparasite activity and anticancer activity. The invention also relates to this peptide as an antiparasite agent, for example in the treatment of toxoplasmosis and as an antic

Evaluation of functional groups on amino acids in cyclic tetrapeptides in histone deacetylase inhibition

The naturally occurring cyclic tetrapeptide, chlamydocin, originally isolated from fungus Diheterospora chlamydosphoria, consists of α-aminoisobutyric acid, l-phenylalanine, d-proline and an unusual amino acid (S)-2-amino-8-((S)-oxiran-2-yl)-8-oxooctanoic acid (Aoe) and inhibits the histone deacetylases (HDACs), a class of regulatory enzymes. The epoxyketone moiety of Aoe is the key functional group for inhibition. The cyclic tetrapeptide scaffold is supposed to play important role for effective binding to the surface of enzymes. In place of the epoxyketone group, hydroxamic acid and sulfhydryl group have been applied to design inhibitor ligands to zinc atom in catalytic site of HDACs. In the research for more potent HDAC inhibitors, we replaced the epoxyketone moiety of Aoe with different functional groups and synthesized a series of chlamydocin analogs as HDAC inhibitors. Among the functional groups, methoxymethylketone moiety showed as potent inhibition as the hydroxamic acid. On the contrary, we confirmed that borate, trifruoromethylketone, and 2-aminoanilide are almost inactive in HDAC inhibition.

Chlamydocin-hydroxamic acid analogues as histone deacetylase inhibitors

Chlamydocin-hydroxamic acid analogues were designed and synthesized as histone deacetylase (HDAC) inhibitors based on the structure and HDAC inhibitory activity of chlamydocin and trichostatin A. Chlamydocin is a cyclic tetrapeptide containing an epoxyketone moiety in the side chain that makes it an irreversible inhibitor of HDAC. We replaced the epoxyketone moiety of chlamydocin with hydroxamic acid to design potent and reversible inhibitors of HDAC. In addition, a number of amino-cycloalkanecarboxylic acids (Acc) are introduced instead of the simple amino-isobutric acid (Aib) for a variety of the series of chlamydocin analogues. The compounds synthesized were tested for HDAC inhibitory activity and the results showed that many of them are potent inhibitors of HDAC. The replacement of Aib residue of chlamydocin with an aromatic amino acid enhances the in vivo and in vitro inhibitory activity. We have carried out circular dichroism and molecular modeling studies on chlamydocin-hydroxamic acid analogue and compared it with the solution structure of chlamydocin.