Fmoc-L-glutamic acid
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Fmoc-L-glutamic acid

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N-Fmoc-L-glutamic acid is an N-Fmoc-protected form of L-Glutamic acid. L-Glutamic acid is a non-essential amino acid that is important to the mammalian central nervous system. L-Glutamic acid is also a neurotransmitter for cone photoreceptors in the human brain and is used as a treatment for patients who have liver disease accompanied by encephalopathy (a condition termed 'hepatic coma').

Fmoc-Amino Acids
Catalog number
CAS number
Molecular Formula
Molecular Weight
Fmoc-L-glutamic acid
Fmoc-L-Glu-OH; N-(9H-Fluorene-9-ylmethoxycarbonyl)-L-glutamic acid; N-Fmoc-L-glutamic AcidFmoc-Glu-OH; (S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)pentanedioic acid; N-Fmoc-L-glutamic Acid; FMOC-GLU-OH
White powder
≥ 98% (HPLC)
1.366±0.06 g/cm3
Melting Point
188-194 °C
Boiling Point
635.8±50.0 °C
Store at 2-8 °C
InChI Key
Canonical SMILES
1.Friendly strategy to prepare encoded one bead-one compound cyclic peptide library.
Giudicessi SL1, Gurevich-Messina JM, Martínez-Ceron MC, Erra-Balsells R, Albericio F, Cascone O, Camperi SA. ACS Comb Sci. 2013 Oct 14;15(10):525-9. doi: 10.1021/co400039a. Epub 2013 Sep 6.
One bead-one peptide libraries allow the screening of suitable ligands for any target protein. Short cyclic peptides are ideal ligands for affinity chromatography because of their high affinity and selectivity for the target protein and stability against proteases. We designed a library synthesis strategy to facilitate the identification of cyclic peptides by MS consisting of (a) sequential incorporation of a mixture of Fmoc-Ala-OH and Fmoc-Asp[2-phenylisopropyl (OPp)]-OH (15:85) to Gly-oxymethylbenzamide-ChemMatrix (Gly-HMBA-CM) resin, (b) synthesis of the combinatorial library on the resin by the divide-couple-recombine method, (c) removal of OPp with 4% TFA, (d) peptide cyclization on solid phase through side-chain Asp and amino terminus, and (e) removal of side chain protecting groups with a 95% TFA cocktail. Peptides were cleaved from the beads with ammonia and the linear code was sequenced by MALDI-TOF MS/MS. The high capacity of ChemMatrix resin together with the sensitivity of MS allows code sequencing from a single bead.
2.A reversible protection strategy to improve Fmoc-SPPS of peptide thioesters by the N-Acylurea approach.
Mahto SK1, Howard CJ, Shimko JC, Ottesen JJ. Chembiochem. 2011 Nov 4;12(16):2488-94. doi: 10.1002/cbic.201100472. Epub 2011 Sep 12.
C-terminal peptide thioesters are an essential component of the native chemical ligation approach for the preparation of fully or semisynthetic proteins. However, the efficient generation of C-terminal thioesters by Fmoc solid-phase peptide synthesis remains a challenge. The recent N-acylurea approach to thioester synthesis relies on the deactivation of one amine of 3,4-diaminobenzoic acid (Dbz) during Fmoc SPPS. Here, we demonstrate that this approach results in the formation of side products through the over-acylation of Dbz, particularly when applied to Gly-rich sequences. We find that orthogonal allyloxycarbonyl (Alloc) protection of a single Dbz amine eliminates these side products. We introduce a protected Fmoc-Dbz(Alloc) base resin that may be directly used for synthesis with most C-terminal amino acids. Following synthesis, quantitative removal of the Alloc group allows conversion to the active N-acyl-benzimidazolinone (Nbz) species, which can be purified and converted in situ to thioester under ligation conditions.
3.Convenient synthesis of collagen-related tripeptides for segment condensation.
Ellison AJ1, VanVeller B1, Raines RT1,2. Biopolymers. 2015 Nov;104(6):674-81. doi: 10.1002/bip.22700.
Chromatography is a common step in the solution-phase synthesis of typical peptides, as well as peptide fragments for subsequent coupling on a solid support. Combining known reagents that form readily separable byproducts is shown to eliminate this step, which wastes time and other resources. Specifically, activating carboxyl groups with isobutyl chloroformate or as pentafluorophenyl esters and using N-methyl morpholine as a base enable chromatography-free synthetic routes in which peptide products are isolated from byproducts by facile evaporation, extraction, and trituration. This methodology was used to access tripeptides related to collagen, such as Fmoc-Pro-Pro-Gly-OH and Fmoc-Pro-Hyp(tBu)-Gly-OH, in a purity suitable for solid-phase segment condensation to form collagen mimetic peptides. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 104: 674-681, 2015.
4.Femtomolar Ln(III) affinity in peptide-based ligands containing unnatural chelating amino acids.
Niedźwiecka A1, Cisnetti F, Lebrun C, Delangle P. Inorg Chem. 2012 May 7;51(9):5458-64. doi: 10.1021/ic300448y. Epub 2012 Apr 10.
The incorporation of unnatural chelating amino acids in short peptide sequences leads to lanthanide-binding peptides with a higher stability than sequences built exclusively from natural residues. In particular, the hexadentate peptide P(22), which incorporates two unnatural amino acids Ada(2) with aminodiacetate chelating arms, showed picomolar affinity for Tb(3+). To design peptides with higher denticity, expected to show higher affinity for Ln(3+), we synthesized the novel unnatural amino acid Ed3a(2) which carries an ethylenediamine triacetate side-chain and affords a pentadentate coordination site. The synthesis of the derivative Fmoc-Ed3a(2)(tBu)(3)-OH, with appropriate protecting groups for direct use in the solid phase peptide synthesis (Fmoc strategy), is described. The two high denticity peptides P(HD2) (Ac-Trp-Ed3a(2)-Pro-Gly-Ada(2)-Gly-NH(2)) and P(HD5) (Ac-Trp-Ada(2)-Pro-Gly-Ed3a(2)-Gly-NH(2)) led to octadentate Tb(3+) complexes with femtomolar stability in water.
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