206759-97-9

Upstream product

• 71989-18-9 Fmoc-Glu(OtBu)-OH 
• 1117-97-1 N,0-dimethylhydroxylamine 
• 153815-59-9 4-(9H-fluoren-9-ylmethoxycarbonylamino)-5-hydroxy-pentanoic acid tert-butyl ester 
• 222639-57-8 γ-tert-butyl α-S-ethyl (S)-N-(fluorenylmethoxycarbonyl)thioglutamate 
• 160002-62-0 (S)-4-Benzylsulfanylcarbonyl-4-(9H-fluoren-9-ylmethoxycarbonylamino)-butyric acid tert-butyl ester 

Downstream Products

• 1383854-82-7 C₄₆H₇₀N₈O₈ 
• 1383854-84-9 C₇₂H₁₁₁N₁₃O₁₂ 
• 1287745-42-9 C₃₃H₃₈N₂O₆ 
• 1287745-87-2 C₃₅H₄₀N₂O₇ 
• 1287745-60-1 C₄₂H₄₆N₂O₇ 

Relevant academic research and scientific papers

Modulating Angiogenesis by Proteomimetics of Vascular Endothelial Growth Factor

Angiogenesis, formation of new blood vessels from the existing vascular network, is a hallmark of cancer cells that leads to tumor vascular proliferation and metastasis. This process is mediated through the binding interaction of VEGF-A with VEGF receptor

Β?CATENIN/ B-CELL LYMPHOMA 9 PROTEIN?PROTEIN INTERACTION INHIBITING PEPTIDOMIMETICS

Disclosed herein is a series of helical sulfono-γ-AApeptides that mimic the binding mode of the α-helical HD2 domain of B-Cell Lymphoma 9 (BCL9). As disclosed herein, sulfono-γ-AApeptides can structurally and functionally mimic the α-helical domain of BCL9, and selectively disrupt β?catenin/BCL9 PPIs with even higher potency. More intriguingly, these sulfono-γ-AApeptides can enter cancer cells, bind with β?catenin and disrupt β?catenin/BCL PPI, and exhibit excellent cellular activity, which is much more potent than the BCL9 peptide. Furthermore, enzymatic stability studies demonstrated the remarkable stability of the helical sulfono-γ-AApeptides, with no degradation in the presence of pronase for 24 h, augmenting their biological potential.

α-Helix-Mimicking Sulfono-γ-AApeptide Inhibitors for p53-MDM2/MDMX Protein-Protein Interactions

The use of peptidomimetic scaffolds is a promising strategy for the inhibition of protein-protein interactions (PPIs). Herein, we demonstrate that sulfono-γ-AApeptides can be rationally designed to mimic the p53 α-helix and inhibit p53-MDM2 PPIs. The best

Design and synthesis of irreversible inhibitors of foot-and-mouth disease virus 3C protease

Foot-and-mouth disease virus (FMDV) causes a highly infectious and economically devastating disease of livestock. The FMDV genome is translated as a single polypeptide precursor that is cleaved into functional proteins predominantly by the highly conserve

Comparison of backbone modification in protein β-sheets by α→γ residue replacement and α-residue methylation

The mimicry of protein tertiary structure by oligomers with unnatural backbones is a significant contemporary research challenge. Among common elements of secondary structure found in natural proteins, sheets have proven the most difficult to address. Here, we report the systematic comparison of different strategies for peptide backbone modification in β-sheets with the goal of identifying the best method for replacing a multi-stranded sheet in a protein tertiary fold. The most effective sheet modifications examined led to native-like tertiary folding behavior with a thermodynamic folded stability comparable to the prototype protein on which the modified backbones are based. This journal is the Partner Organisations 2014.

N-Acylpolyamine inhibitors of HDM2 and HDMX binding to p53

Selective inhibition of protein-protein interactions important for cellular processes could lead to the development of new therapies against disease. In the area of cancer, overexpression of the proteins human double minute 2 (HDM2) and its homolog HDMX has been linked to tumor aggressiveness. Both HDM2 and HDMX bind to p53 and prevent cell cycle arrest or apoptosis in damaged cells. Developing a strategy to simultaneously prevent the binding of both HDM2 and HDMX to p53 is an essential feature of inhibitors to restore p53 activity in a number of different cancers. Inhibition of protein-protein interactions with synthetic molecules is an emerging area of research that requires new inhibitors tailored to mimic the types of interfaces between proteins. Our strategy to create inhibitors of protein-protein interactions is to develop a non-natural scaffold that may be used as a starting point to identify important molecular components necessary for inhibition. In this study, we report an N-acylpolyamine (NAPA) scaffold that supports numerous sidechains in a compact atomic arrangement. NAPAs were constructed by a series of reductive aminations between amino acid derivatives followed by acylation at the resulting secondary amine. An optimized NAPA was able to equally inhibit the association of both HDM2 and HDMX with p53. Our results demonstrate some of the challenges associated with targeting multiple protein-protein interactions involved in overlapping cellular processes.

DMSO-aided o-iodoxybenzoic acid (IBX) oxidation of Fmoc-protected amino alcohols

A fast and highly convenient procedure for the formation of Fmoc-protected amino aldehydes from the corresponding alcohols using 1.1 equiv. of IBX in the presence of dimethylsulfoxide (DMSO) is discussed. This procedure leads to the clean synthesis of Fmo

Melanocortin receptor-specific compounds

A melanocortin receptor-specific compound of the general formula of structure I: where X, R1, R2a, R2b, R3, R4a, R4b, R5a and R5b are as defined in the specification,