106665-76-3

Upstream product

• 41324-66-7 H-Pro-OBzl 
• 13734-41-3 t-Boc-L-valine 
• 58872-03-0 1--L-valyl>-L-proline phenylmethyl ester 

Downstream Products

• 1233764-72-1 C₂₉H₃₄N₄O₅ 
• 1324010-61-8 C₂₇H₃₆N₄O₃ 
• 1324010-60-7 C₂₇H₃₆N₄O₃ 
• 1186650-55-4 C₂₁H₃₂N₄O₃ 
• 99429-46-6 Val-Val-Pro-OBzl 
• 504431-33-8 Boc-Gly-Ile-Gly-Val-Pro-ONp 
• 504431-32-7 Boc-Gly-Leu-Gly-Val-Pro-ONp 
• 504431-30-5 Boc-Gly-Ile-Gly-Val-Pro-OBzl 
• 504431-29-2 Boc-Gly-Leu-Gly-Val-Pro-OBzl 
• 99429-45-5 Boc-Val-Val-Pro-OBzl 

Relevant academic research and scientific papers

Design and synthesis of tryptophan containing peptides as potential analgesic and anti-inflammatory agents

A new series of smaller peptides with tryptophan at C-terminal and varying N-protected amino acids/peptides were designed, synthesized and characterized by analytical and spectroscopic techniques. Analgesic and anti-inflammatory properties of these peptides were carried out in vivo using tail-flick method and carrageenan-induced paw edema method, respectively, at different doses and different time intervals. Most of the peptides synthesized displayed enhanced activity, and particularly tetra and hexapeptides 29-31 were found to be even more potent than the reference standards used. Moreover, some peptides have exhibited promising activity even after 24h of administration, whereas the reference standards were active only up to 3h. Further, the compounds did not present any ulcerogenic liability.

Design, synthesis and evaluation of monovalent Smac mimetics that bind to the BIR2 domain of the anti-apoptotic protein XIAP

We report the systematic rational design and synthesis of new monovalent Smac mimetics that bind preferentially to the BIR2 domain of the anti-apoptotic protein XIAP. Characterization of compounds in vitro (including 9i; ML101) led to the determination of key structural requirements for BIR2 binding affinity. Compounds 9h and 9j sensitized TRAIL-resistant breast cancer cells to apoptotic cell death, highlighting the value of these probe compounds as tools to investigate the biology of XIAP.

Hydrophobicity profile of amino acid residues: A differential scanning calorimetry and circular dichroism study of leucine and isoleucine co-polypeptides of the protein-based polymers of elastin

The inverse temperature transition of hydrophobic folding and assembly of a "host-guest" model system based on the elastin derived polypentapeptide, poly(VPGVG), is employed to determine the relative hydrophobicity of amino acid residues of proteins and p