942518-21-0

Basic information

• Product Name: FMoc-Hpg-OH
• Synonyms: FMoc-HoMoGly(Propargyl)-OH;FMoc-Hpg-OH;(2S)-2-[[(9H-Fluoren-9-ylmethoxy)carbonyl]amino]-5-hexynoic acid;Fmoc-L-propargylalanine;Fmoc-L-homopropargylglycine;(2S)-2-(Fmoc-amino)-5-hexynoic acid;5-Hexynoic acid, 2-[[(9H-fluoren-9- ylmethoxy)carbonyl]amino]-, (2S)-;(9H-Fluoren-9-yl)MethOxy]Carbonyl HomoGly(Propargyl)-OH
• CAS NO: 942518-21-0
• Molecular Formula: C₂₁H₁₉NO₄
• Molecular Weight: 349.37986
• EINECS: -0
• Product Categories: Unusual Amino Acids;amino acids
• Mol File: 942518-21-0.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 585.7±50.0 °C(Predicted)
• Appearance: /
• Density: 1.265±0.06 g/cm3(Predicted)
• PKA: 3.73±0.10(Predicted)
• CAS DataBase Reference: FMoc-Hpg-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMoc-Hpg-OH(942518-21-0)
• EPA Substance Registry System: FMoc-Hpg-OH(942518-21-0)

Safety Data

• Hazardous Substances Data: 942518-21-0(Hazardous Substances Data)

Usage

General Description

FMoc-Hpg-OH, also known as N-(9H-Fluoren-9-ylmethoxycarbonyl)-L-homophenylglycine, is a chemical compound commonly used in peptide synthesis. FMoc-Hpg-OH is a derivative of homophenylglycine, an amino acid that is not found in natural proteins but can be a useful tool in the design and synthesis of peptidomimetics. FMoc-Hpg-OH is often used as a building block in solid-phase peptide synthesis due to its stability and ease of manipulation. It can be coupled with other amino acids to form peptide chains and is commonly used in the production of peptides for research and pharmaceutical applications.

Upstream product

• 38771-21-0 4-bromobut-1-yne 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 102774-86-7 9-fluorenylmethyl N-succinimidyl carbonate 
• 98891-36-2 (S)-2-amino-5-hexynoic acid 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 

Relevant articles and documents

An Optimized Synthesis of Fmoc- l -Homopropargylglycine-OH

An efficient multigram synthesis of alkynyl amino acid Fmoc-l-homopropargylglycine-OH is described. A double Boc protection is optimized for high material throughput, and the key Seyferth-Gilbert homologation is optimized to avoid racemization. Eighteen grams of the enantiopure (>98% ee) noncanonical amino acid was readily generated for use in solid phase synthesis to make peptides that can be functionalized by copper-assisted alkyne-azide cycloaddition.

Design of triazole-stapled BCL9 α-helical peptides to target the β-catenin/B-cell CLL/lymphoma 9 (BCL9) protein-protein interaction

The interaction between β-catenin and B-cell CLL/lymphoma 9 (BCL9), critical for the transcriptional activity of β-catenin, is mediated by a helical segment from BCL9 and a large binding groove in β-catenin. Design of potent, metabolically stable BCL9 peptides represents an attractive approach to inhibit the activity of β-catenin. In this study, we report the use of the Huisgen 1,3-dipolar cycloaddition reaction to generate triazole-stapled BCL9 α-helical peptides. The high efficiency and mild conditions of this "click" reaction combined with the ease of synthesis of the necessary unnatural amino acids allows for facile synthesis of triazole-stapled peptides. We have performed extensive optimization of this approach and identified the optimal combinations of azido and alkynyl linkers necessary for stapling BCL9 helices. The unsymmetrical nature of the triazole staple also allowed the synthesis of double-stapled BCL9 peptides, which show a marked increase in helical character and an improvement in binding affinity and metabolic stability relative to wild-type and linear BCL9 peptides. This study lays the foundation for further optimization of these triazole-stapled BCL9 peptides as potent, metabolically stable, and cell-permeable inhibitors to target the β-catenin and BCL9 interaction.