146803-41-0

Basic information

• Product Name: FMOC-ALA-ALDEHYDE
• Synonyms: FMOC-ALA-ALDEHYDE;(S)-(9H-fluoren-9-yl)methyl 1-oxopropan-2-ylcarbamate;(9H-Fluoren-9-yl)MethOxy]Carbonyl Ala-aldehyde
• CAS NO: 146803-41-0
• Molecular Formula: C₁₈H₁₇NO₃
• Molecular Weight: 295.33
• Mol File: 146803-41-0.mol
• Article Data: 29

Chemical Properties

• Boiling Point: 479.9±28.0 °C(Predicted)
• Appearance: /
• Density: 1.203±0.06 g/cm3(Predicted)
• Storage Temp.: Inert atmosphere,Store in freezer, under -20°C
• PKA: 10.80±0.46(Predicted)
• CAS DataBase Reference: FMOC-ALA-ALDEHYDE(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-ALA-ALDEHYDE(146803-41-0)
• EPA Substance Registry System: FMOC-ALA-ALDEHYDE(146803-41-0)

Safety Data

• Hazard Codes: N
• Statements: 50
• Safety Statements: 61
• Hazardous Substances Data: 146803-41-0(Hazardous Substances Data)

Usage

Uses

Fmoc-ala-aldehyde acts as an intermediate in the synthesis of α-amino aldehydes and peptide aldehydes.

Upstream product

• 35661-39-3 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 1117-97-1 N,0-dimethylhydroxylamine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 146346-88-5 methyl 2-(((9H-fluoren-9-yl)methoxy)carbonyl)aminopropanoate 
• 198542-03-9 (9H-fluoren-9-yl)methyl (S)-(1-(methoxy(methyl)amino)-1-oxopropan-2-yl)carbamate 
• 161529-13-1 (S)-2-(N-fluorenylmethoxycarbonylamino)propanol 
• 103321-50-2 9H-fluoren-9-ylmethyl [(1S)-2-chloro-1-methyl-oxoethyl]carbamate 
• 125814-20-2 Fmoc-L-Ala-NCA 

Downstream Products

• 762232-44-0 benzyl N-(2-Fmoc-amino-L-methylethyl)glycinate 
• 382149-37-3 {[2-(9H-fluoren-9-ylmethoxycarbonylamino)-propyl]-[(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-acetyl]-amino}-acetic acid benzyl ester 
• 382149-22-6 {[2-(2-{[2-(9H-fluoren-9-ylmethoxycarbonylamino)-propyl]-[(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-acetyl]-amino}-acetylamino)-propyl]-[(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-acetyl]-amino}-acetic acid benzyl ester 
• 948888-01-5 4(S)-[(9-fluorenylmethoxycarbonyl)amino]-2-pentenoic acid benzyl ester 
• 1447194-67-3 benzyl (4S)-4-(N-fmoc)-amino-3-oxopentanoate 
• 1447194-82-2 C₃₅H₃₂N₄O₅S₂ 
• 1447194-77-5 benzyl 4-[(1S)-1-(N-fmoc)aminoethyl]-2-methyl-1,3-thiazole-5-carboxylate 
• 1447195-24-5 C₄₂H₃₈N₄O₅S₂ 
• 1383854-83-8 C₄₄H₆₈N₈O₆ 
• 1311399-87-7 FmocNH-L-Ala-ψ[C3H3NO]-CO-NH Phe-COOMe 

Relevant articles and documents

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

Solid-phase synthesis of peptide vinyl sulfones as potential inhibitors and activity-based probes of cysteine proteases

(Matrix presented) Peptide vinyl sulfones were prepared from 2-chlorotrityl resin-bound phenolic amino vinyl sulfones in high yield and purity. This method enables the convenient synthesis of peptide vinyl sulfones having different amino acids at the Psu

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.