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Application Area

Fmoc-L-aspartic acid β-benzyl ester

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

Fmoc-Amino Acids

Catalog number

BAT-003744

CAS number

86060-84-6

Molecular Formula

C26H23NO6

Molecular Weight

445.50

IUPAC Name

(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-oxo-4-phenylmethoxybutanoic acid

Synonyms

Fmoc-L-Asp(OBzl)-OH; (2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-oxo-4-phenylmethoxybutanoic acid; N-Alpha-Fmoc-L-aspartic acid beta-benzyl ester

Appearance

White powder

Purity

≥ 98% (HPLC)

Density

1.310±0.06 g/cm3

Melting Point

122-126 °C

Boiling Point

687.2±55.0 °C

Storage

Store at 2-8 °C

InChI

InChI=1S/C26H23NO6/c28-24(32-15-17-8-2-1-3-9-17)14-23(25(29)30)27-26(31)33-16-22-20-12-6-4-10-18(20)19-11-5-7-13-21(19)22/h1-13,22-23H,14-16H2,(H,27,31)(H,29,30)/t23-/m0/s1

InChI Key

OQGAELAJEGGNKG-QHCPKHFHSA-N

Canonical SMILES

C1=CC=C(C=C1)COC(=O)CC(C(=O)O)NC(=O)OCC2C3=CC=CC=C3C4=CC=CC=C24

Fmoc-L-aspartic acid β-benzyl ester is a chemical compound primarily used in the field of peptide synthesis. The Fmoc (9-fluorenylmethoxycarbonyl) group is a protective moiety used to safeguard the amino group during synthesis. This ester form of aspartic acid is strategically utilized due to its ability to maintain structural integrity and facilitate the introduction of side-chain functionalities. Its usage is critical in the creation of complex peptides, ensuring that the synthesis proceeds with high efficiency and accuracy. The compound’s design allows for easy removal of the Fmoc group under mildly basic conditions, preserving the sensitive peptide linkages and enabling subsequent synthetic steps.

The first key application area of Fmoc-L-aspartic acid β-benzyl ester is in the realm of pharmaceutical research and development. Peptides play a crucial role in the design of novel drugs, particularly in targeting specific biological pathways and interactions. This compound aids in the synthesis of therapeutic peptides, which can act as enzyme inhibitors, hormones, or receptor agonists/antagonists. By enabling the precise assembly of amino acid sequences, it supports the development of peptide-based drugs with improved stability, efficacy, and specificity. This enhancement in peptide synthesis is pivotal in accelerating the drug discovery process and tailoring treatments for various diseases.

Another significant application of Fmoc-L-aspartic acid β-benzyl ester is in the creation of biomaterials. Peptide-based biomaterials are gaining traction for their biocompatibility and functionality in medical applications, including tissue engineering and regenerative medicine. The compound facilitates the construction of peptide hydrogels, scaffolds, and coatings that can mimic the extracellular matrix and support cell adhesion, proliferation, and differentiation. By fine-tuning the peptide sequences, researchers can design materials with specific mechanical properties and bioactivities, aiding in the development of innovative solutions for wound healing, bone regeneration, and soft tissue repair.

Furthermore, Fmoc-L-aspartic acid β-benzyl ester is employed in biochemical research to study protein-protein interactions and enzyme mechanics. Peptide models derived from this compound serve as crucial tools in elucidating the structural and functional aspects of proteins. By incorporating specific residues into peptides, scientists can investigate how modifications affect protein binding and activity, offering insights into fundamental biological processes. These studies are instrumental in advancing our understanding of diseases linked to protein misfolding and aggregation, such as neurodegenerative disorders.

Lastly, the compound is used in the synthesis of customized peptides for diagnostic purposes. These tailored peptides can function as probes in various assays, aiding in the detection and quantification of biomarkers associated with different diseases. The specificity and high fidelity of Fmoc-based peptide synthesis allow for the creation of diagnostic tools with enhanced sensitivity and selectivity. Such applications are crucial in early disease detection and monitoring, providing valuable information for both clinical diagnosis and research. By leveraging these peptides, scientists and healthcare professionals can improve diagnostic accuracy and ultimately enhance patient outcomes.

1.Structural study of poly(beta-benzyl-L-aspartate) monolayers at air-liquid interfaces.

Riou SA1, Hsu SL, Stidham HD. Biophys J. 1998 Nov;75(5):2451-60.

As normally studied, in the solid state or in solution, poly(beta-benzyl-L-aspartate) (PBLA) differs from the other helical polyamino acids in that its alpha-helical conformation is most stable in the left-handed rather than in the right-handed form. The slightly lower energy per residue for the left-handed form in PBLA is easily perturbed, however. The helical screw sense can be inverted in a polar environment and, upon heating above 100 degrees C, a distorted left-handed helix or omega-helix is irreversibly formed. From external reflectance Fourier transform infrared measurements at the air-water interface, the conformation of PBLA in the monolayer state is directly established for the first time. The infrared frequencies of the amide bands suggest that right-handed alpha-helices are formed on the surface of water immediately after spreading the monolayers and independently of the polypeptide conformational distribution in the spreading solution.

2.Solvolysis and aminolysis on peptidyl-Kaiser oxime resin assisted by Ca2+ and Eu3+: a mild procedure to prepare alpha-methyl and -ethyl esters of protected peptides.

Moraes CM1, Bemquerer MP, Miranda MT. J Pept Res. 2000 Apr;55(4):279-88.

Ca2+ and Eu3+ were able to assist solvolysis on peptidyl-Kaiser oxime resins generating alpha-methyl and -ethyl esters of protected peptides. The methanolysis assistance was at least twice as effective as that of acetic acid, the common catalyst used in aminolysis of the ester oxime linkage. No molar excess of Ca2+ or Eu3+ was needed to enhance this reaction efficiency. Ca2+ also assisted aminolysis on peptidyl-Kaiser oxime resins. Solvolysis and aminolysis rates depended on the nature of the C-terminal residue attached to the resin and on the alcohol used. Both reactions were selective to the ester oxime linkage since no significant amount of secondary products, resulting from rearrangements or simultaneous transesterification of the beta-benzyl or cyclohexyl esters, was detected in the reaction media. The alpha-methyl and -ethyl esters of Ac-Ala-Gly-X [where, X = Gly, Ala, Phe or Lys (2-Cl-Z)] and of Ac-Ile-Ser (Bzl)-Asp(OZ) (where, Z = Bzl or cHex) were essentially the only products formed in the solvolyses performed.

3.Transport of amino acid-based prodrugs by the Na+- and Cl(-) -coupled amino acid transporter ATB0,+ and expression of the transporter in tissues amenable for drug delivery.

Hatanaka T1, Haramura M, Fei YJ, Miyauchi S, Bridges CC, Ganapathy PS, Smith SB, Ganapathy V, Ganapathy ME. J Pharmacol Exp Ther. 2004 Mar;308(3):1138-47. Epub 2003 Nov 14.

We evaluated the potential of the Na(+)- and Cl(-)-coupled amino acid transporter ATB(0,+) as a delivery system for amino acid-based prodrugs. Immunofluorescence analysis indicated that ATB(0,+) is expressed abundantly on the luminal surface of cells lining the lumen of the large intestine and the airways of the lung and in various ocular tissues, including the conjunctival epithelium, the tissues easily amenable for drug delivery. We screened a variety of beta-carboxyl derivatives of aspartate and gamma-carboxyl derivatives of glutamate as potential substrates for this transporter using heterologous expression systems. In mammalian cells expressing the cloned ATB(0,+), several of the aspartate and glutamate derivatives inhibited glycine transport via ATB(0,+). Direct evidence for ATB(0,+)-mediated transport of these derivatives was obtained in Xenopus laevis oocytes using electrophysiological methods. Exposure of oocytes, which express ATB(0,+) heterologously, to aspartate beta-benzyl ester as a model derivative induced inward currents in a Na(+)- and Cl(-)-dependent manner with a Na(+)/Cl(-)/aspartate beta-benzyl ester stoichiometry of 2:1:1.

4.1,4-diazepine-2,5-dione ring formation during solid phase synthesis of peptides containing aspartic acid beta-benzyl ester.

Süli-Vargha H1, Schlosser G, Ilas J. J Pept Sci. 2007 Nov;13(11):742-8.

The Fmoc-based SPPS of H-Xaa-Asp(OBzl)-Yaa-Gly-NH(2) sequences results in side reactions yielding not only aspartimide peptides and piperidide derivatives, but also 1,4-diazepine-2,5-dione-peptides. Evidence is presented to show that the 1,4-diazepine-2,5-dione derivative is formed from the aspartimide peptide. The rate of this ring transformation depends primarily on the tendency to aspartimide and piperidide formation, which is influenced by the nature of the amino acid following the aspartic acid beta-benzyl ester (Xaa). However the bulkiness of the amino acid side chain preceeding the aspartic acid beta-benzyl ester (Yaa) is also important. Under certain conditions the 1,4-diazepine-2,5-dione peptide derivative may even be formed dominantly, which is a highly undesirable side reaction in peptide synthesis, but which provides a new way for the synthesis of diazepine peptide derivatives with targeted biological or pharmacological activity.