299207-24-2

Upstream product

• 35661-40-6 N-Fmoc L-Phe 
• 6638-79-5 N,O-dimethylhydroxylamine*hydrochloride 
• 1117-97-1 N,0-dimethylhydroxylamine 
• 103321-57-9 2S-flouren-9-ylmethoxycarbonylamino-3-phenylpropionyl chloride 

Downstream Products

• 1326776-54-8 C₂₈H₂₉NO₄ 
• 1447195-24-5 C₄₂H₃₈N₄O₅S₂ 
• 1447195-39-2 C₅₂H₅₆N₈O₇S₄ 
• 1447194-69-5 benzyl (4S)-4-(N-fmoc)amino-3-oxo-5-phenylpentanoate 
• 1447194-84-4 C₃₂H₃₆N₄O₅S₂ 
• 1447194-98-0 benzyl 4-[(1S)-1-(N-fmoc)amino-2-phenethyl]-2-methyl-1,3-thiazole-5-carboxylate 
• 1447195-12-1 C₂₀H₂₀N₂O₂S 
• 1447194-80-0 C₂₇H₂₈N₄O₃S₂ 
• 1447194-82-2 C₃₅H₃₂N₄O₅S₂ 

Relevant academic research and scientific papers

Probing α-Amino Aldehydes as Weakly Acidic Pronucleophiles: Direct Access to Quaternary α-Amino Aldehydes by an Enantioselective Michael Addition Catalyzed by Br?nsted Bases

The high tendency of α-amino aldehydes to undergo 1,2-additions and their relatively low stability under basic conditions have largely prevented their use as pronucleophiles in the realm of asymmetric catalysis, particularly for the production of quaternary α-amino aldehydes. Herein, it is demonstrated that the chemistry of α-amino aldehydes may be expanded beyond these limits by documenting the first direct α-alkylation of α-branched α-amino aldehydes with nitroolefins. The reaction produces densely functionalized products bearing up to two, quaternary and tertiary, vicinal stereocenters with high diastereo- and enantioselectivity. DFT modeling leads to the proposal that intramolecular hydrogen bonding between the NH group and the carbonyl oxygen atom in the starting α-amino aldehyde is key for reaction stereocontrol.

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

Rational Design of Right-Handed Heterogeneous Peptidomimetics as Inhibitors of Protein-Protein Interactions

Peptidomimetics have gained great attention for their function as protein-protein interaction (PPI) inhibitors. Herein, we report the design and investigation of a series of right-handed helical heterogeneous 1:1 α/Sulfono-I-AA peptides as unprecedented inhibitors for p53-MDM2 and p53-MDMX. The most potent helical heterogeneous 1:1 α/Sulfono-I-AA peptides were shown to bind tightly to MDM2 and MDMX, with Kd of 19.3 and 66.8 nM, respectively. Circular dichroism spectra, 2D-NMR spectroscopy, and the computational simulations suggested that these helical sulfono-I-AA peptides could mimic the critical side chains of p53 and disrupt p53/MDM2 PPI effectively. It was noted that these 1:1 α/Sulfono-I-AA peptides were completely resistant to proteolytic degradation, boosting their potential for biomedical applications. Furthermore, effective cellular activity is achieved by the stapled 1:1 α/Sulfono-I-AA peptides, evidenced by significantly enhanced p53 transcriptional activity and much more induced level of MDM2 and p21. The 1:1 α/Sulfono-I-AA peptides could be an alternative strategy to antagonize a myriad of PPIs.

Synthesis and biological activity of peptide α-ketoamide derivatives as proteasome inhibitors

Proteasome activity affects cell cycle progression as well as the immune response, and it is largely recognized as an attractive pharmacological target for potential therapies against several diseases. Herein we present the synthesis of a series of pseudo

One-pot synthesis of Weinreb amides employing 3,3-dichloro-1,2-diphenylcyclopropene (CPI-Cl) as a chlorinating agent

The synthesis of Nα-protected amino alkyl Weinreb amides starting from the corresponding α-amino acids as well as carboxylic acids has been delineated through the in situ generation of acid chlorides using CPI-Cl as a chlorinating agent. The protocol is simple; the reaction conditions employed were mild, and compatible with all the three commonly used urethane protecting groups namely, Boc, Cbz and Fmoc groups. The resulting Weinreb amides are obtained in good yields as optically pure products.

Helical oligomers of thiazole-based γ-amino acids: Synthesis and structural studies

9-Helix: 4-Amino(methyl)-1,3-thiazole-5-carboxylic acids (ATCs) were synthesized as new γ-amino acid building blocks. The structures of various ATC oligomers were analyzed in solution by CD and NMR spectroscopy and in the solid state by X-ray crystallography. The ATC sequences adopted a well-defined 9-helix structure in the solid state and in aprotic and protic organic solvents as well as in aqueous solution. Copyright

Efficient synthesis of N-protected amino/peptide Weinreb amides from T3P and DBU

The reaction of Nα-protected amino/peptide acid with N,O-dimethylhydroxylamine hydrochloride in the presence of T3P and DBU to obtain enantiomerically pure Nα-protected amino/peptidyl Weinreb amides in high yields has been described. Fmoc-Ala-Weinreb amide 2a is obtained as single crystal, and its structure was determined through X-ray crystallography.

A peptide aldehyde microarray for high-throughput profiling of cellular events

Microarrays provide exciting opportunities in the field of large-scale proteomics. With the aim to elucidate enzymatic activity and profiles within native biological samples, we developed a microarray comprising a focused positional-scanning library of enzyme inhibitors. The library was diversified across P1-P4 positions, creating 270 different inhibitor sublibraries which were immobilized onto avidin slides. The peptide aldehyde-based small-molecule microarray (SMM) specifically targeted cysteine proteases, thereby enabling large-scale functional assessment of this subgroup of proteases, within fluorescently labeled samples, including pure proteins, cellular lysates, and infected samples. The arrays were shown to elicit binding fingerprints consistent with those of model proteins, specifically caspases and purified cysteine proteases from parasites (rhodesein and cruzain). When tested against lysates from apoptotic Hela and red blood cells infected with Plasmodium falciparum, clear signatures were obtained that were readily attributable to the activity of constituent proteases within these samples. Characteristic binding profiles were further able to distinguish various stages of the parasite infection in erythrocyte lysates. By converting one of our brightest microarray hits into a probe, putative protein markers were identified and pulled down from within apoptotic Hela lysates, demonstrating the potential of target validation and discovery. Taken together, these results demonstrate the utility of targeted SMMs in dissecting cellular biology in complex proteomic samples.

Asymmetric syntheses of α-methyl γ-amino acid derivatives

This project was undertaken to demonstrate the potential of asymmetric hydrogenations mediated by the chiral, carbene-oxazoline analogue of Crabtree's catalyst "cat" in asymmetric hydrogenations of allylic amine derivatives of amino acids. Peripheral feat

Elaboration of peptidomimetics derived from a PADAM approach: Synthesis of polyfunctionalised 2(1H)-pyrazinones via an unexpected aromatisation

When the PADAM (Passerini reaction-amine deprotection-acyl migration) strategy is applied to N-Boc amino acids, the resulting β-acylamino- α-hydroxyamides can be elaborated by secondary-alcohol oxidation, Boc deprotection, and intramolecular cyclisation.