175452-89-8

Usage

Uses

Used in Pharmaceutical Research and Development:
N-Fmoc-D-Glutamic acid 1-methyl ester is used as a building block for the synthesis of pharmaceuticals, bioconjugates, and other biologically active molecules. The N-Fmoc protective group allows for selective deprotection and efficient coupling reactions, facilitating the creation of complex peptide structures.
Used in Solid-Phase Peptide Synthesis:
In the field of solid-phase peptide synthesis, N-Fmoc-D-Glutamic acid 1-methyl ester is used as a key component to construct peptides with specific sequences. The methyl ester group provides stability and protection against unwanted side reactions, ensuring the successful synthesis of the desired peptide.

Upstream product

• 368443-68-9 α-methyl γ-allyl (2R)-N-(fluoren-9-ylmethoxycarbonyl)glutamate 
• 204251-33-2 γ-allyl (2R)-N-(fluoren-9-ylmethoxycarbonyl)glutamate 

Downstream Products

• 195302-00-2 β-allyl (2S)-N-(fluoren-9-ylmethoxycarbonyl)phenylalanyl-β-alanyl-[α-methyl (2R)-glutamyl]-γ-(2S)-prolyl-[α-methyl (2R)-aspartate] triester 
• 368443-70-3 (2S)-N-(fluoren-9-ylmethoxycarbonyl)phenylalanyl-β-alanyl-[α-methyl (2R)-glutamyl]-γ-(2S)-prolyl-[α-methyl (2R)-aspartic acid] 
• 368449-14-3 cyclo[-(2S,3S,E)-2-methyl-3-phenylethenyl-3-aminopropanoyl-β-(R)-Glu-α-OMe-γ-(S)-Pro-(R)-Asp-α-OMe-β-(S)-Phe-] 
• 368449-08-5 cyclo[-(3R,E)-3-phenylethenyl-3-aminopropanoyl-α-(R)-Glu-α-OMe-γ-Sar-(R)-Asp-α-OMe-β-(S)-Phe-] 
• 368449-09-6 cyclo[-(2S,3S,E)-2-methyl-3-phenylethenyl-3-aminopropanoyl-α-(R)-Glu-α-OMe-γ-Sar-(R)-Asp-α-OMe-β-(S)-Phe-] 
• 195302-01-3 (2S)-phenylalanyl-β-alanyl-[α-methyl (2R)-glutamyl]-γ-(2S)-prolyl-[α-methyl (2R)-aspartate] diester 

Relevant academic research and scientific papers

Design and preparation of serine-threonine protein phosphatase inhibitors based upon the nodularin and microcystin toxin structures. Part 3

Nodularin and microcystins are complex natural cyclic isopeptidic hepatotoxins that serve as subnanomolar inhibitors of the eukaryotic serine-threonine protein phosphatases PP1 and PP2A, enzymes that are intimately involved in controlling cellular metabolism. Previously we described a solution-phase synthesis of stripped-down nodularin analogues; cyclo[-β-Ala-(R)-Glu-α-OMe-γ-Sar-(R)-Asp-α-OMe- β-(S)-Phe-] 3 and cyclo[-(3R)-3-hydroxymethyl-β-Ala-(R)-Glu-α-OMe-γ-Sar-(R)- Asp-α-OMe-β-(S)-Phe-] 5. The synthetic strategy was designed to allow post-macrocyclisation elaboration. Here we examine alternative methods for introducing diversity and achieving macrolactamisation and compare the relative efficiency of solution- vs. solid-phase peptide syntheses of the macrocycles. Syntheses and the biological activities of the macrocycles cyclo{-[(2R)-α-4-benzylpiperidinylamido-Asp]-β-[(R)-Glu]-γ- Sar-[(R)-Asp]-β-(S)-Phe-} 29 and cyclo{-(2S)-Phe-[(2R)-α-4-benzylpiperidinylamido-Asp]-(R)-Glu-γ- (S)-Pro-β-(R)-Asp-} 65 are compared. Both compounds contain sufficient side-chain functionality to interact with a hydrophobic groove at the enzyme active site. The proline containing analogues 30, 31 (R3 = CH3) where sarcosine is replaced in macrocycles 3 and 4, were also synthesised in order to correlate conformational properties with biological activity. In accord with predictions macrocycles 29 and 65 were found to be weak inhibitors of PP1 with IC50 2.9 and 2.7 mM respectively.