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Application Area

Boc-D-aspartic acid α-amide

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

Category

BOC-Amino Acids

Catalog number

BAT-002706

CAS number

200282-47-9

Molecular Formula

C9H16N2O5

Molecular Weight

232.24

IUPAC Name

(3R)-4-amino-3-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxobutanoic acid

Synonyms

Boc-D-Asp-NH2; Boc-D-isoasparagine; (R)-4-Amino-3-((tert-butoxycarbonyl)amino)-4-oxobutanoic acid

Appearance

Off-white powder

Purity

≥ 98%

Density

1.253±0.06 g/cm3(Predicted)

Melting Point

103-109 °C

Boiling Point

462.7±40.0 °C(Predicted)

Storage

Store at 2-8°C

InChI

InChI=1S/C9H16N2O5/c1-9(2,3)16-8(15)11-5(7(10)14)4-6(12)13/h5H,4H2,1-3H3,(H2,10,14)(H,11,15)(H,12,13)/t5-/m1/s1

InChI Key

VKCARTLEXJLJBZ-RXMQYKEDSA-N

Canonical SMILES

CC(C)(C)OC(=O)NC(CC(=O)O)C(=O)N

Boc-D-aspartic acid α-amide, a protected amino acid derivative widely utilized in peptide synthesis, plays a pivotal role in various applications. Here are four key applications presented with high perplexity and burstiness:

Peptide Synthesis: Acting as a cornerstone in the intricate process of synthesizing complex peptides, Boc-D-aspartic acid α-amide is indispensable. Its protective Boc group shields against undesired side reactions during peptide assembly, ensuring precision. Upon completion of synthesis, the Boc group can be effortlessly cleaved, yielding the desired peptide sequence with exceptional purity, exemplifying the meticulous craftsmanship involved in peptide construction.

Drug Development: In the realm of pharmaceutical exploration, Boc-D-aspartic acid α-amide takes center stage in crafting peptide-based drug candidates. These tailored peptides are engineered to target specific disease-related receptors or enzymes, showcasing the precision afforded by incorporating Boc-D-aspartic acid α-amide. By manipulating the structure and characteristics of therapeutic peptides, researchers pave the way for innovative drug development strategies with potential therapeutic breakthroughs.

Bioconjugation: Embracing the versatility of Boc-D-aspartic acid α-amide, bioconjugation techniques leverage its capabilities to tether peptides to diverse biomolecules or surfaces. This strategic utilization is instrumental in developing cutting-edge diagnostic tools, targeted drug delivery systems, and biosensors. The Boc protecting group ensures the aspartic acid residue remains reactive, facilitating controlled conjugation processes that underscore the finesse of bioconjugation applications.

Structural Biology: In the intricate domain of structural biology, Boc-D-aspartic acid α-amide emerges as a key player in unraveling the intricate relationships between protein structure and function. By synthesizing peptides that emulate specific protein segments, researchers delve into the influence of distinct amino acid sequences on protein folding and stability. This profound understanding of protein structure-function dynamics not only sheds light on essential biological mechanisms but also propels the design of novel protein-based therapeutics into uncharted territories of innovation and discovery.

1. Methods for syntheses of N-methyl-DL-aspartic acid derivatives

M Boros, J Kökösi, J Vámos, I Kövesdi, B Noszál Amino Acids. 2007 Nov;33(4):709-17. doi: 10.1007/s00726-006-0453-4. Epub 2007 Mar 2.

A novel practical method for the synthesis of N-methyl-DL-aspartic acid 1 (NMA) and new syntheses for N-methyl-aspartic acid derivatives are described. NMA 1, the natural amino acid was synthesized by Michael addition of methylamine to dimethyl fumarate 5. Fumaric or maleic acid mono-ester and -amide were regioselectively transformed into beta-substituted aspartic acid derivatives. In the cases of maleamic 11a or fumaramic esters 11b, the alpha-amide derivative 13 was formed, but hydrolysis of the product provided N-methyl-DL-asparagine 9 via base catalyzed ring closure to DL-alpha-methylamino-succinimide 4, followed by selective ring opening. Efficient methods were developed for the preparation of NMA-alpha-amide 13 from unprotected NMA via sulphinamide anhydride 15 and aspartic anhydride 3 intermediate products. NMA diamide 16 was prepared from NMA dimethyl ester 6 and methylamino-succinimide 4 by ammonolysis. Temperature-dependent side reactions of methylamino-succinimide 4 led to diazocinone 18, resulted from self-condensation of methylamino-succinimide via nucleophyl ring opening and the subsequent ring-transformation.

2. Synthesis of antimicrobial peptoids

Paul R Hansen, Jens K Munk Methods Mol Biol. 2013;1047:151-9. doi: 10.1007/978-1-62703-544-6_11.

Peptoids (N-substituted glycines) are mimics of α-peptides in which the side chains are attached to the backbone N (α) -amide nitrogen instead of the C (α) -atom. Peptoids hold promise as therapeutics since they often retain the biological activity of the parent peptide and are stable to proteases. In recent years, peptoids have attracted attention as new potential antibiotics against multiresistant bacteria. Here we describe the submonomer solid-phase synthesis of an antimicrobial peptoid, H-Nmbn-Nlys-Nlys-Nnap-Nbut-Nmbn-Nlys-NH2.

3. Alteration of substrate specificity of aspartase by directed evolution

Yasuhisa Asano, Ikuo Kira, Kenzo Yokozeki Biomol Eng. 2005 Jun;22(1-3):95-101. doi: 10.1016/j.bioeng.2004.12.002.

Aspartase (l-aspartate ammonia-lyase, EC 4.3.1.1), which catalyzes the reversible deamination of l-aspartic acid to yield fumaric acid and ammonia, is highly selective towards l-aspartic acid. We screened for enzyme variants with altered substrate specificity by a directed evolution method. Random mutagenesis was performed on an Escherichia coli aspartase gene (aspA) by error-prone PCR to construct a mutant library. The mutant library was introduced to E. coli and the transformants were screened for production of fumaric acid-mono amide from l-aspartic acid-alpha-amide. Through the screening, one mutant, MA2100, catalyzing deamination of l-aspartic acid-alpha-amide was achieved. Gene analysis of the MA2100 mutant indicated that the mutated enzyme had a K327N mutation. The characteristics of the mutated enzyme were examined. The optimum pH values for the l-aspartic acid and l-aspartic acid-alpha-amide of the mutated enzyme were pH 8.5 and 6.0, respectively. The K(m) value and V(max) value for the l-aspartic acid of the mutated enzyme were 28.3 mM and 0.26 U/mg, respectively. The K(m) value and V(max) value for the l-aspartic acid-alpha-amide of the mutated enzyme were 1450 mM and 0.47 U/mg, respectively. This is the first report describing the alteration of the substrate specificity of aspartase, an industrially important enzyme.