Fmoc-L-glutamine 4-nitrophenyl ester
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Fmoc-L-glutamine 4-nitrophenyl ester

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Category
Fmoc-Amino Acids
Catalog number
BAT-003765
CAS number
71989-21-4
Molecular Formula
C26H23N3O7
Molecular Weight
489.50
Fmoc-L-glutamine 4-nitrophenyl ester
IUPAC Name
(4-nitrophenyl) (2S)-5-amino-2-(9H-fluoren-9-ylmethoxycarbonylamino)-5-oxopentanoate
Synonyms
Fmoc-L-Gln-ONp; (4-nitrophenyl)(2S)-5-amino-2-(9H-fluoren-9-ylmethoxycarbonylamino)-5-oxopentanoate
Purity
≥ 95%
Density
1.362 g/cm3
Storage
Store at 2-8 °C
InChI
InChI=1S/C26H23N3O7/c27-24(30)14-13-23(25(31)36-17-11-9-16(10-12-17)29(33)34)28-26(32)35-15-22-20-7-3-1-5-18(20)19-6-2-4-8-21(19)22/h1-12,22-23H,13-15H2,(H2,27,30)(H,28,32)/t23-/m0/s1
InChI Key
KLCANCMZDAZCCW-QHCPKHFHSA-N
Canonical SMILES
C1=CC=C2C(=C1)C(C3=CC=CC=C32)COC(=O)NC(CCC(=O)N)C(=O)OC4=CC=C(C=C4)[N+](=O)[O-]

Fmoc-L-glutamine 4-nitrophenyl ester, a versatile chemical reagent, plays a pivotal role in peptide synthesis and biochemical research. Here are four key applications of this compound:

Peptide Synthesis: Serving as a fundamental component in peptide synthesis, Fmoc-L-glutamine 4-nitrophenyl ester acts as a crucial protected amino acid intermediate. Its Fmoc group, known for its exceptional stability, is particularly well-suited for solid-phase peptide synthesis techniques. Through the strategic incorporation of this ester into peptide chains, researchers can methodically construct intricate peptide sequences endowed with specific functional groups, showcasing precise control over molecular design and assembly.

Protein Engineering: Within the realm of protein engineering, Fmoc-L-glutamine 4-nitrophenyl ester assumes a vital role in introducing glutamine residues into protein sequences. By harnessing esterified amino acids, researchers can exert precise influence over protein folding dynamics and structural stability, leading to the creation of proteins with tailored functionalities and enhanced properties. This intricate manipulation of amino acid compositions facilitates the design of proteins optimized for diverse industrial or therapeutic applications.

Drug Development: In the domain of drug development, Fmoc-L-glutamine 4-nitrophenyl ester emerges as a key player in the synthesis of peptide-based pharmaceuticals. Through targeted modifications of peptide backbones using specific amino acid esters, researchers can enhance drug stability and bioavailability, elevating the therapeutic potential of these compounds. This strategic approach enables the generation of novel therapeutic peptides characterized by heightened efficacy and improved longevity within the biological milieu, underscoring the compound’s significance in advancing pharmaceutical innovation and personalized medicine.

Chemical Biology: Within the realm of chemical biology research, Fmoc-L-glutamine 4-nitrophenyl ester serves as a valuable tool for investigating protein-protein interactions and elucidating enzyme functions. Through its integration into peptide substrates or inhibitors, scientists gain access to the active sites of enzymes and the binding interfaces of proteins, offering critical insights into molecular recognition processes and catalytic mechanisms. This molecular interrogation serves as the foundation for comprehending complex biological pathways and holds promise for designing tailored molecules capable of modulating these interactions for therapeutic interventions, embodying a sophisticated interplay between chemical design and biological function.

1. Thrombin inhibition by the highly selective 'reversible suicide substrate' N-ethoxycarbonyl-D-phenylalanyl-L-prolyl-alpha-azalysine p-nitrophenyl ester
Paolo Ascenzi, Carlo Gallina, Martino Bolognesi Protein Pept Lett. 2005 Jul;12(5):433-8. doi: 10.2174/0929866054395301.
Thrombin is the last enzyme in the blood coagulation cascade. All pharmacological aspects support the use of thrombin inhibitors as antithrombotic agents. Here, we review the unusual inhibition behavior of the highly selective 'reversible suicide substrate' N-ethoxycarbonyl-D-phenylalanyl-L-prolyl-alpha-azalysine p-nitrophenyl ester (Eoc-D-Phe-Pro-azaLys-ONp) targeted to the active center of human alpha-thrombin. Eoc-D-Phe-Pro-azaLys-ONp is an acylating agent, but its hydrolysis product 1(N-ethoxycarbonyl-D-phenylalanyl-L-prolyl)-2(4-aminobutyl) hydrazine behaves as a highly selective human alpha-thrombin competitive inhibitor.
3. β-Glucuronidase-coupled assays of glucuronoyl esterases
Lucia Fraňová, Vladimír Puchart, Peter Biely Anal Biochem. 2016 Oct 1;510:114-119. doi: 10.1016/j.ab.2016.07.023. Epub 2016 Jul 22.
Glucuronoyl esterases (GEs) are microbial enzymes with potential to cleave the ester bonds between lignin alcohols and xylan-bound 4-O-methyl-d-glucuronic acid in plant cell walls. This activity renders GEs attractive research targets for biotechnological applications. One of the factors impeding the progress in GE research is the lack of suitable substrates. In this work, we report a facile preparation of methyl esters of chromogenic 4-nitrophenyl and 5-bromo-4-chloro-3-indolyl β-D-glucuronides for qualitative and quantitative GE assay coupled with β-glucuronidase as the auxiliary enzyme. The indolyl derivative affording a blue indigo-type product is suitable for rapid and sensitive assay of GE in commercial preparations as well as for high throughput screening of microorganisms and genomic and metagenomic libraries.
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