221186-79-4

Upstream product

• 162757-06-4 Z-L-Phe-D-Pro-OtBu 
• 1161-13-3 N-Cbz-L-Phe 
• 184719-80-0 D-proline tert-butyl ester hydrochloride 
• 2812-46-6 L-proline t-butyl ester 
• 201206-00-0 Z-D-Pro-OtBu 

Downstream Products

• 162757-03-1 BocLys(Z)-Aib-Phe-(D)ProOtBu 
• 561039-31-4 (R)-1-{(S)-2-[(1-Benzyloxycarbonylamino-cyclohexanecarbonyl)-amino]-3-phenyl-propionyl}-pyrrolidine-2-carboxylic acid tert-butyl ester 
• 1000593-27-0 cyclo(-L-7-bromo-Ahp-Aib-L-Phe-D-Pro-) 
• 291312-78-2 H-L-Asu(OBzl)-Aib-L-Phe-D-Pro-OH TFA salt 
• 1380236-99-6 C₃₄H₅₃BrN₄O₇ 
• 1380237-00-2 C₂HF₃O₂*C₂₅H₃₇BrN₄O₅ 
• 1011725-85-1 C₂₈H₄₂N₄O₆ 
• 1011725-65-7 scyclo [L-2-amino-8-oxoundecanoyl-aminoisobutyryl-L-phenylalanyl-D-prolyl] 

Relevant academic research and scientific papers

Design and synthesis of CHAP31, trapoxin B and HC-toxin based bicyclic tetrapeptides disulfide as potent histone deacetylase inhibitors

The naturally occurring cyclic depsipeptide, FK228 inhibits histone deacetylase (HDAC) enzymes after reductive cleavage of intra-molecular disulfide bond. One of the sulfhydryl groups produced in the reduction interacts with zinc atom that involved in the

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.

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 analogs bearing carbonyl group as possible ligand toward zinc atom in histone deacetylases

A series of chlamydocin analogs with various carbonyl functionalities were designed and synthesized as histone deacetylase (HDAC) inhibitors. Chlamydocin is a cyclic tetrapeptide containing an epoxyketone surrogate in the side chain which makes it irrever

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.

Synthesis of new cytotoxic cyclopeptide analogs of Chlamodycin

With the aim of discovering new antitumoral compounds, analogs of Chlamodycin and HC toxin containing biologically active groups have been designed and synthesized.Interesting preliminary results concerning the in vitro cytotoxic activity of some of these