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Application Area

Fmoc-L-aspartic acid-α-tert-butylester

* 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-003747

CAS number

129460-09-9

Molecular Formula

C23H25NO6

Molecular Weight

411.50

IUPAC Name

(3S)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-4-[(2-methylpropan-2-yl)oxy]-4-oxobutanoic acid

Synonyms

Fmoc-L-Asp-OtBu; L-Fmoc-Aspartic acid α-tert-butyl ester; 1-tert-Butyl N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-L-aspartate; fmoc-asp-otbu; Fmoc-L-aspartic acid 1-tert-butyl ester

Appearance

White powder

Purity

≥ 99.5% (Chiral HPLC)

Density

1.251±0.06 g/cm3

Melting Point

100-118 °C

Boiling Point

617.4±55.0 °C

Storage

Store at 2-8 °C

InChI

InChI=1S/C23H25NO6/c1-23(2,3)30-21(27)19(12-20(25)26)24-22(28)29-13-18-16-10-6-4-8-14(16)15-9-5-7-11-17(15)18/h4-11,18-19H,12-13H2,1-3H3,(H,24,28)(H,25,26)/t19-/m0/s1

InChI Key

VZXQYACYLGRQJU-IBGZPJMESA-N

Canonical SMILES

CC(C)(C)OC(=O)C(CC(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13

Fmoc-L-aspartic acid-α-tert-butylester, often abbreviated as Fmoc-Asp(OtBu)-OH, is a derivative of aspartic acid, a naturally occurring amino acid. It is a key reagent used in peptide synthesis, especially in the solid-phase peptide synthesis (SPPS) method. The Fmoc (9-fluorenylmethoxycarbonyl) group is a protective group that shields the amino group of the aspartic acid during the synthesis process. This protection is essential to ensure that the peptide chain elongates correctly without unwanted side reactions. The α-tert-butylester group, on the other hand, is a protecting group for the carboxyl group of aspartic acid, which prevents it from reacting prematurely. The combination of these groups makes Fmoc-L-aspartic acid-α-tert-butylester a crucial tool in the precise assembly of peptides and proteins in the lab.

One of the primary industrial applications of Fmoc-L-aspartic acid-α-tert-butylester is in the pharmaceutical industry, where it is used for the synthesis of peptide-based drugs. Peptides often serve as therapeutic agents due to their high specificity and efficacy in targeting biological systems. Fmoc-L-aspartic acid-α-tert-butylester aids in creating complex peptide sequences required for these drugs, ensuring their purity and functionality. The precision offered by this reagent is vital for developing new medications with minimal side effects.

Another significant application is in the production of peptide-based materials for research and development. Scientists and researchers use Fmoc-L-aspartic acid-α-tert-butylester to create custom peptides for various studies, including the development of new diagnostic tools and biosensors. These peptides can be used to study protein interactions, enzyme functions, and cellular processes, making this reagent an indispensable part of the research toolkit.

Fmoc-L-aspartic acid-α-tert-butylester also plays a role in the development of high-performance biomaterials. In materials science, peptides synthesized using this reagent can be incorporated into biomaterials for medical implants and tissue engineering. The stability and biocompatibility of these peptides make them suitable for creating advanced materials that interact favorably with biological tissues. This application highlights the versatility of Fmoc-L-aspartic acid-α-tert-butylester beyond traditional peptide synthesis.

Finally, this reagent is utilized in the creation of specialty chemicals and catalysts. The peptides synthesized with Fmoc-L-aspartic acid-α-tert-butylester can act as catalysts in various chemical reactions or be used as intermediates in the production of other chemical products. This application underscores the reagent's role in enabling complex chemical processes and the creation of innovative products across different industries.

1.Synthesis of beta- and gamma-fluorenylmethyl esters of respectively N alpha-Boc-L-aspartic acid and N alpha-Boc-L-glutamic acid.

al-Obeidi F1, Sanderson DG, Hruby VJ. Int J Pept Protein Res. 1990 Mar;35(3):215-8.

The orthogonal synthesis of N alpha-Boc-L-aspartic acid-gamma-fluorenylmethyl ester and N alpha-Boc-L-glutamic acid-delta-fluorenylmethyl ester is reported. This is a four-step synthesis that relies on the selective esterification of the side-chain carboxyl groups on N alpha-CBZ-L-aspartic acid and N alpha-CBZ-L-glutamic acid. Such selectivity is accomplished by initially protecting the alpha-carboxyl group through the formation of the corresponding 5-oxo-4-oxazolidinone ring. Following side-chain esterification, the alpha-carboxyl and alpha-amino groups are deprotected with acidolysis. Finally, the alpha-amino group is reprotected with the t-butyl-oxycarbonyl (Boc) group. Thus aspartic acid and glutamic acid have their side-chain carboxyl groups protected with the base-labile fluorenylmethyl ester (OFm) and their alpha-amino groups protected with the acid-labile Boc group. These residues, when used in conjunction with N alpha-Boc-N epsilon-Fmoc-L-lysine, are important in the formation of side-chain to side-chain cyclizations, via an amide bridge, during solid-phase peptide synthesis.

2.A 'conovenomic' analysis of the milked venom from the mollusk-hunting cone snail Conus textile--the pharmacological importance of post-translational modifications.

Bergeron ZL1, Chun JB, Baker MR, Sandall DW, Peigneur S, Yu PY, Thapa P, Milisen JW, Tytgat J, Livett BG, Bingham JP. Peptides. 2013 Nov;49:145-58. doi: 10.1016/j.peptides.2013.09.004. Epub 2013 Sep 18.

Cone snail venoms provide a largely untapped source of novel peptide drug leads. To enhance the discovery phase, a detailed comparative proteomic analysis was undertaken on milked venom from the mollusk-hunting cone snail, Conus textile, from three different geographic locations (Hawai'i, American Samoa and Australia's Great Barrier Reef). A novel milked venom conopeptide rich in post-translational modifications was discovered, characterized and named α-conotoxin TxIC. We assign this conopeptide to the 4/7 α-conotoxin family based on the peptide's sequence homology and cDNA pre-propeptide alignment. Pharmacologically, α-conotoxin TxIC demonstrates minimal activity on human acetylcholine receptor models (100 μM, <5% inhibition), compared to its high paralytic potency in invertebrates, PD50 = 34.2 nMol kg(-1). The non-post-translationally modified form, [Pro](2,8)[Glu](16)α-conotoxin TxIC, demonstrates differential selectivity for the α3β2 isoform of the nicotinic acetylcholine receptor with maximal inhibition of 96% and an observed IC50 of 5.

3.Synthesis of an amino acid analogue to incorporate p-aminobenzyl-EDTA in peptides.

Song AI1, Rana TM. Bioconjug Chem. 1997 Mar-Apr;8(2):249-52.

A convenient and straightforward synthesis of an amino acid analog, [p-(N-alpha-Fmoc-L-aspartic acid-beta-amido)benzyl]-EDTA tetra-tert-butyl ester, compatible with Fmoc solid phase peptide synthesis strategy is described. This reagent was used to incorporate p-aminobenzyl-EDTA at an internal sequence position in an HIV-1 Tat protein fragment. After cleavage from the resin and standard deprotection, the peptide was purified by high-performance liquid chromatography and characterized by mass spectrometry. Through this methodology, flexible linkers of different lengths and containing various structures can be placed between the alpha-carbon backbone of peptides and metal chelates. These peptides will provide a new class of affinity cleaving reagents that can be directed against protein and nucleic acid targets.