1370442-74-2

Upstream product

• 1000593-27-0 cyclo(-L-7-bromo-Ahp-Aib-L-Phe-D-Pro-) 
• 10387-40-3 potassium thioacetate 
• 30992-29-1 Boc-Aib-OH 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 64472-06-6 (R)-proline benzyl ester 
• 221186-79-4 (+)-(R)-tert-butyl 1-[(S)-2-amino-3-phenylpropanoyl]pyrrolidine-2-carboxylate 
• 162757-06-4 Z-L-Phe-D-Pro-OtBu 
• 2812-46-6 L-proline t-butyl ester 
• 1161-13-3 N-Cbz-L-Phe 
• 1429340-58-8 (-)-(S)-butyl 2-{2-[(tert-butoxycarbonyl)amino]hex-5-enamido}-2-methylpropanoate 
• 92136-57-7 (S)-2-tert-butoxycarbonylamino-hex-5-enoic acid methyl ester 
• 208522-13-8 (S)-2-N-(tert-butoxycarbonyl)-2-amino-5-hexenoic acid 
• 507-09-5 tiolacetic acid 
• 1429340-69-1 (+)-(S)-butyl 2-{2-[(tert-butoxycarbonyl)amino]hept-6-enamido}-2-methylpropanoate 

Downstream Products

• 1380239-15-5 C₂₅H₃₆N₄O₄S 
• 952196-95-1 cyclo [L-2-amino-7-(2-pyridyldithio)heptanoyl-aminoisobutyryl-luaranyl-D-prolyl] 

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.

Synthesis, evaluation and molecular modeling of cyclic tetrapeptide histone deacetylase inhibitors as anticancer agents

Histone deacetylase inhibitors (HDACIs) are a promising class of anticancer agents. To examine whether a slight change in the recognition domain could alter their inhibitory activity, we synthesized a series of cyclo(-l-Am7(S2Py)-Aib-l-Phe(n-Me)-d-Pro)derivatives and evaluated their HDAC inhibitory and anticancer activities. The peptides exhibited potent HDAC inhibitory activity and inhibited three human cancer cell lines with IC50 in the micromolar range. Docking and molecular dynamics simulation were conducted to explore the interaction mechanisms of class I and II HDACs with these inhibitors. It revealed that the zinc ion in the active site coordinated five atoms of HDACs and the sulfur atom of the inhibitor. The metal binding domains of these compounds interacted with HDAC2, and the surface recognition domains of these compounds interacted with HDAC4 through hydrogen bonding. The hydrophobic interactions also provided favorable contributions to stabilize the complexes. The results obtained from this study would be helpful for us to design some novel cyclic tetrapeptides that may act as potent HDACIs.