940301-35-9

Basic information

• Product Name: FMOC-(2S,3R)-2-AMINO-3-HYDROXY-4-METHYLPENTANOIC ACID
• Synonyms: FMOC-(2S,3R)-2-AMINO-3-HYDROXY-4-METHYLPENTANOIC ACID;(2S,3R)-2-(FMOC-AMINO)-3-HYDROXY-4-METHYLPENTANOIC ACID
• CAS NO: 940301-35-9
• Molecular Formula: C₂₁H₂₃NO₅
• Molecular Weight: 369.41
• Product Categories: unnatural amino acids
• Mol File: 940301-35-9.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 601.8±55.0 °C(Predicted)
• Appearance: /
• Density: 1.271±0.06 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• PKA: 3.51±0.23(Predicted)
• CAS DataBase Reference: FMOC-(2S,3R)-2-AMINO-3-HYDROXY-4-METHYLPENTANOIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-(2S,3R)-2-AMINO-3-HYDROXY-4-METHYLPENTANOIC ACID(940301-35-9)
• EPA Substance Registry System: FMOC-(2S,3R)-2-AMINO-3-HYDROXY-4-METHYLPENTANOIC ACID(940301-35-9)

Safety Data

• Hazardous Substances Data: 940301-35-9(Hazardous Substances Data)

Usage

General Description

FMoc-(2S,3R)-2-amino-3-hydroxy-4-methylpentanoic acid is a chemical compound commonly used in the field of peptide synthesis. It is a derivative of the amino acid leucine, with a modified structure that includes a fluorophenylmethyloxycarbonyl (FMoc) protecting group. The compound is important for the creation of peptide chains, as its unique structure allows for precise control over the addition of amino acids and the formation of peptide bonds. It is widely used in the production of custom peptides for research purposes, as well as in the development of pharmaceutical drugs and biotechnology products.

Upstream product

• 5817-22-1 (2S,3R)-3-hydroxyleucine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 102774-86-7 9-fluorenylmethyl N-succinimidyl carbonate 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 

Downstream Products

• 940301-25-7 Boc-D-Leu-L-Leu-L-threo-O-[L-Ser(OtBu)]-HyPhe-L-Leu(OTBS)-L-Leu-OAll 
• 940301-24-6 Boc-D-Leu-L-Leu-L-threo-O-[Fmoc-L-Ser(OtBu)]-HyPhe-L-HyLeu(OTBS)-L-Leu-OAll 
• 940301-23-5 Boc-D-Leu-L-Leu-L-HyPhe-L-HyLeu(OTBS)-L-Leu-OAll 

Relevant articles and documents

Deciphering Specificity Determinants for FR900359-Derived Gqα Inhibitors Based on Computational and Structure–Activity Studies

Direct targeting of intracellular Gα subunits of G protein-coupled receptors by chemical tools is a challenging task in current pharmacological studies and in the development of novel therapeutic approaches. In this study we analyzed novel FR900359-based analogs from natural sources, synthetic cyclic peptides, as well as all so-far known Gqα inhibitors in a comprehensive study to devise a strategy for the elucidation of characteristics that determine interactions with and inhibition of Gq in the specific FR/YM-binding pocket. Using 2D NMR spectroscopy and molecular docking we identified unique features in the macrocyclic structures responsible for binding to the target protein correlating with inhibitory activity. While all novel compounds were devoid of effects on Gi and Gs proteins, no inhibitor surpassed the biological activity of FR. This raises the question of whether depsipeptides such as FR already represent valuable chemical tools for specific inhibition of Gq and, at the same time, are suitable natural lead structures for the development of novel compounds to target Gα subunits other than Gq.

Total synthesis of lysobactin

Antibiotic resistance has become a significant public health concern. Antibiotics that belong to new structural classes and manifest their biological activity via novel mechanisms are urgently needed. Lysobactin, a depsipeptide antibiotic has displayed very strong antibacterial activity against methicillin-resistant Staphylococcus aureus (MRSA) as well as vancomycin-resistant enterococci (VRE) with minimum inhibitory concentrations (MICs) ranging from 0.39 to 0.78 μg/mL. The MIC values against VRE were more than 50-fold lower than those reported for vancomycin itself. Lysobactin was found to inhibit nascent peptidoglycan formation; however, this activity was not antagonized in the presence of N-acyl-L-Lys-D-Ala-D-Ala, the binding domain on the cell wall precursors that is utilized by vancomycin. Thus, lysobactin represents a promising agent for the treatment bacterial infections due to resistant pathogens. We describe a convergent synthesis of lysobactin that relies upon a highly efficient macrocyclization reaction to assemble the 28-membered cyclic depsipeptide. This synthesis provides the foundation for further study of the mode of action utilized by lysobactin and its analogues.