276672-36-7

Upstream product

• 1125-88-8 benzaldehyde dimethyl acetal 
• 35661-51-9 N-(9-fluorenylmethyloxycarbonyl)hydrazine 
• 1111765-75-3 C₂₂H₁₈N₂O₂ 
• 147688-35-5 C₂₇H₂₈N₂O₄ 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 555-96-4 Benzylhydrazine 
• 100-52-7 benzaldehyde 

Downstream Products

• 861851-75-4 1-Fmoc-2-benzyl-4-(o-chlorobenzyl)semicarbazide 

Relevant academic research and scientific papers

Aza-amino acid scanning of chromobox homolog 7 (CBX7) ligands

An aza-amino acid scan of peptide inhibitors of the chromobox homolog 7 (CBX7) was performed to study the conformational requirements for affinity to the methyllysine reader protein. Twelve azapeptide analogues were prepared using three different approaches employing respectively N-(Fmoc)aza-amino acid chlorides and submonomer azapeptide synthesis to install systematically aza-residues at the first four residues of the peptide, as well as to provide aza-lysine residues possessing saturated and unsaturated side chains. The aza-peptide ligands were evaluated in a chromobox homolog 7 binding assay, providing useful insight into structural requirements for affinity. Copyright

Azapeptides as CD36 binding compounds

An azapeptide compound of Formula I: A-(Xaa)a-N(RA)—N(RB)—C(O)-(Xaa′)b-B??I.

CYCLIC AZAPEPTIDES AS INTEGRIN MARKERS

The present application is directed to radiolabeled cyclic polyazapeptides, pharmaceutical compositions comprising radiolabeled cyclic polyazapeptides, and methods of using the radiolabeled cyclic polyazapeptides. Such polyazapeptides can be used in imaging studies, such as Positron Emitting Tomography (PET) or Single Photon Emission Computed Tomography (SPECT).

Cyclic aza-peptide integrin ligand synthesis and biological activity

Aza-peptides are obtained by replacement of the α-C-atom of one or more amino acids by a nitrogen atom in a peptide sequence. Introduction of aza-residues into peptide sequences may result in unique structural and pharmacological properties, such that aza-scanning may be used to probe structure-activity relationships. In this study, a general approach for the synthesis of cyclic aza-peptides was developed by modification of strategies for linear aza-peptide synthesis and applied in the preparation of cyclic aza-pentapeptides containing the RGD (Arg-Gly-Asp) sequence. Aza-amino acid scanning was performed on the cyclic RGD-peptide Cilengitide, cyclo[R-G-D-f-N(Me)V] 1, and its parent peptide cyclo(R-G-D-f-V) 2, potent antagonists of the αvβ3, αvβ5, and α5β1 integrin receptors, which play important roles in human tumor metastasis and tumor-induced angiogenesis. Although incorporation of the aza-residues resulted generally in a loss of binding affinity, cyclic aza-peptides containing aza-glycine retained nanomolar activity toward the αvβ3 receptor.

Novel semicarbazide-derived inhibitors of human dipeptidyl peptidase I (hDPPI)

Human dipeptidyl peptidase I (hDPPI, cathepsin C, EC 3.4.14.1) is a novel putative drug target for the treatment of inflammatory diseases. Using 1 as a starting point (IC50 > 10 μM), we have improved potency by more than 500-fold and successfully identified novel inhibitors of DPPI via screening of a one-bead-two-compounds library of semicarbazide derivatives. Selected compounds were shown to inhibit intracellular DPPI in RBL-2H3 cells. These compounds were further characterized for adverse effects on HepG2 cells (cytotoxicity and viability) and their metabolic stability in rat liver microsomes was estimated. One of the most potent inhibitors, 8 (IC50 = 31 ± 3 nM; Ki = 45 ± 2 nM, competitive inhibition), is selective for DPPI over other cysteine and serine proteases, has a half-life of 24 min in rat liver microsomes, shows approximately 50% inhibition of intracellular DPPI at 20 μM and is noncytotoxic.

Symmetry-based HIV protease inhibitors containing (S,S) or (R,R) tartaric acid core structure

Two series of symmetry-based HIV protease inhibitors containing (S,S) or (R,R) tartaric acid core structure were prepared and tested for inhibitory property against the enzyme. All compounds showed weak antiprotease activity.