1365564-57-3

Upstream product

• 1202778-98-0 methyl 2-cyano-3-[4-(trifluoromethyl)phenyl]-2-{[4-(trifluoromethyl)phenyl]methyl}propionate 
• 1365564-15-3 methyl 3-amino-2,2-bis{[p-(trifluoromethyl)phenyl]methyl}propionate 
• 1365564-46-0 C₇H₈O₃S*C₂₀H₁₉F₆NO₂ 
• 1365564-50-6 C₁₉H₁₆F₆NO₂^(1-)*Li⁽¹⁺⁾ 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 402-49-3 4-bromomethyltrifluoromethylbenzene 

Relevant academic research and scientific papers

An amphipathic cyclic tetrapeptide scaffold containing halogenated β2,2-amino acids with activity against multiresistant bacteria

The present study describes the synthesis and biological studies of a small series of head-to-tail cyclic tetrapeptides of the general structure c(Lys-β2,2-Xaa-Lys) containing one lipophilic β2,2-amino acid and Lys, Gly, Ala, or Phe as the Xaa residue in the sequence. The peptides were investigated for antimicrobial activity against gram-positive and gram-negative reference strains and 30 multiresistant clinical isolates including strains with extended spectrum β-lactamase—carbapenemase (ESBL-CARBA) production. Toxicity was determined against human red blood cells. The most potent peptides showed high activity against the gram-positive clinical isolates with minimum inhibitory concentrations of 4–8?μg/mL and low haemolytic activity. The combination of high antimicrobial activity and low toxicity shows that these cyclic tetrapeptides containing lipophilic β2,2-amino acids form a valuable scaffold for designing novel antimicrobial agents.

Synthesis of anticancer heptapeptides containing a unique lipophilic β2,2-amino acid building block

We report a series of synthetic anticancer heptapeptides (H-KKWβ2,2WKK-NH2) containing eight different central lipophilic β2,2-amino acid building blocks, which have demonstrated high efficiency when used as scaffolds in small cationic antimicrobial peptides and peptidomimetics. The most potent peptides in the present study had IC50 values of 9-23μm against human Burkitt's lymphoma and murine B-cell lymphoma and were all nonhaemolytic (EC50>200μm). The most promising peptide 10e also demonstrated low toxicity against human embryonic lung fibroblast cells and peripheral blood mononuclear cells and exceptional proteolytic stability.