940301-35-9

Usage

Uses

Used in Pharmaceutical Development:
FMoc-(2S,3R)-2-amino-3-hydroxy-4-methylpentanoic acid is utilized as a key component in the synthesis of pharmaceutical drugs. Its precise control over peptide chain formation allows for the development of targeted therapies with specific biological activities.
Used in Biotechnology:
In the biotechnology industry, FMoc-(2S,3R)-2-amino-3-hydroxy-4-methylpentanoic acid is employed as a building block for the creation of novel bioactive peptides. These peptides can have applications in areas such as diagnostics, therapeutics, and as components of biosensors.
Used in Research Laboratories:
FMoc-(2S,3R)-2-amino-3-hydroxy-4-methylpentanoic acid is used as a reagent in research settings for the synthesis of custom peptides. This allows scientists to explore the properties and potential applications of new peptide sequences, contributing to the advancement of peptide science.
Used in Peptide Synthesis:
FMoc-(2S,3R)-2-amino-3-hydroxy-4-methylpentanoic acid is used as a protected amino acid in solid-phase peptide synthesis. The FMoc group protects the amino group during the synthesis process, ensuring that only the desired peptide bonds are formed without unwanted side reactions.

Upstream product

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

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 academic research and scientific papers

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 the cyclic depsipeptide YM-280193, a platelet aggregation inhibitor

The first total synthesis of YM-280193, a cyclic depsipeptide that inhibits the ADP-induced aggregation of human platelets, is described. The monomer and dipeptide fragments were prepared using conventional chemistry and subsequently assembled by Fmoc-solid-phase peptide synthesis (Fmoc-SPPS). A late-stage novel bis-alkylation-elimination of cysteine on-resin was employed to introduce the unnatural N-methyldehydroalanine moiety. The final step involved execution of a key macrolactamization reaction between the hindered unnatural N,O-dimethylthreonine and ?2-hydroxyleucine residues.

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.