61533-24-2

Upstream product

• 13734-41-3 t-Boc-L-valine 
• 7672-27-7 N^ω-nitro-L-arginine benzyl ester 

Downstream Products

• 99429-56-8 Boc-Val-Val-Arg(NO₂)-OBzl 
• 1446197-86-9 C₂₁H₃₅N₉O₅ 

Relevant academic research and scientific papers

Design, synthesis and evaluation of inhibitor of apoptosis protein (IAP) antagonists that are highly selective for the BIR2 domain of XIAP

We recently reported the systematic ligand-based rational design and synthesis of monovalent Smac mimetics that bind preferentially to the BIR2 domain of the anti-apoptotic protein XIAP. Expanded structure-activity relationship (SAR) studies around these peptidomimetics led to compounds with significantly improved selectivity (>60-fold) for the BIR2 domain versus the BIR3 domain of XIAP. The potent and highly selective IAP antagonist 8q (ML183) sensitized TRAIL-resistant prostate cancer cells to apoptotic cell death, highlighting the merit of this probe compound as a valuable tool to investigate the biology of XIAP.

Fibrinopeptides. IV. Synthesis of human fibrinopeptide A

Human fibrinopeptide A, a hexadecapeptide, released by the action of thrombin on fibrinogen during clotting of blood, has been synthesized by conventional methods. The synthetic peptide as well as some of the intermediates in the synthesis have been examined for anticoagulant activity. Though all of them were found to be active, the terminal carboxyl protected peptides are more potent inhibitors of clotting than the carboxyl free peptides.