Boc-D-aspartic acid
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Boc-D-aspartic acid

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Category
BOC-Amino Acids
Catalog number
BAT-002705
CAS number
62396-48-9
Molecular Formula
C9H15NO6
Molecular Weight
233.20
Boc-D-aspartic acid
IUPAC Name
(2R)-2-[(2-methylpropan-2-yl)oxycarbonylamino]butanedioic acid
Synonyms
Boc-D-Asp-OH
Appearance
Solid
Purity
≥ 99% (HPLC)
Density
1.302±0.06 g/cm3(Predicted)
Melting Point
116-123 °C
Boiling Point
377.4±32.0 °C(Predicted)
Storage
Store at 2-8°C
InChI
InChI=1S/C9H15NO6/c1-9(2,3)16-8(15)10-5(7(13)14)4-6(11)12/h5H,4H2,1-3H3,(H,10,15)(H,11,12)(H,13,14)/t5-/m1/s1
InChI Key
KAJBMCZQVSQJDE-RXMQYKEDSA-N
Canonical SMILES
CC(C)(C)OC(=O)NC(CC(=O)O)C(=O)O

Boc-D-aspartic acid, a protected derivative of aspartic acid, plays a pivotal role in peptide synthesis and biotechnological research. Explore the diverse applications of Boc-D-aspartic acid presented with high perplexity and burstiness:

Peptide Synthesis: Embracing solid-phase peptide synthesis, Boc-D-aspartic acid emerges as a critical building block for constructing intricate peptides. The Boc (tert-butyloxycarbonyl) group functions as a protective shield, safeguarding against unwanted reactions throughout synthesis. This meticulous process ensures the precise integration of the aspartic acid residue into the peptide chain, orchestrating the creation of complex molecular structures.

Pharmaceutical Development: Positioned at the forefront of pharmaceutical innovation, Boc-D-aspartic acid is a key player in the formulation and manufacturing of peptide-based drugs. Its integration into drug formulations enhances stability, efficacy, and pharmacokinetic properties, elevating the therapeutic potential of these medications. This sophisticated approach reshapes the landscape of drug design, ushering in a new era of pharmaceutical development.

Protein Engineering: In the realm of protein engineering, Boc-D-aspartic acid serves as a potent tool for introducing specific aspartic acid residues into recombinant proteins. By manipulating the protein’s sequence, researchers unravel the intricate role of aspartic acid in protein structure, function, and interactions. This in-depth analysis sheds light on protein stability, paving the way for the design of enhanced protein variants tailored for industrial or therapeutic use.

Enzyme Inhibition Studies: Delving into enzyme inhibition studies, Boc-D-aspartic acid acts as a vital precursor for crafting enzyme inhibitors, especially those targeting aspartic proteases. By incorporating this modified amino acid into inhibitor molecules, scientists delve into the mechanisms of enzyme action, crafting potent inhibitors with precision. These inhibitors play a pivotal role in research endeavors and the development of targeted therapies for disorders characterized by aberrant protease activity.

1.Selective and reversible thiol-pegylation, an effective approach for purification and characterization of five fully active ficin (iso)forms from Ficus carica latex.
Azarkan M1, Matagne A, Wattiez R, Bolle L, Vandenameele J, Baeyens-Volant D. Phytochemistry. 2011 Oct;72(14-15):1718-31. doi: 10.1016/j.phytochem.2011.05.009. Epub 2011 Jun 12.
The latex of Ficus carica constitutes an important source of many proteolytic components known under the general term of ficin (EC 3.4.22.3) which belongs to the cysteine proteases of the papain family. So far, no data on the purification and characterization of individual forms of these proteases are available. An effective strategy was used to fractionate and purify to homogeneity five ficin forms, designated A, B, C, D1 and D2 according to their sequence of elution from a cation-exchange chromatographic support. Following rapid fractionation on a SP-Sepharose Fast Flow column, the different ficin forms were chemically modified by a specific and reversible monomethoxypolyethylene glycol (mPEG) reagent. In comparison with their un-derivatized counterparts, the mPEG-protein derivatives behaved differently on the ion-exchanger, allowing us for the first time to obtain five highly purified ficin molecular species titrating 1mol of thiol group per mole of enzyme.
2.High yielding selective access to spirocyclopropanated 5-oxopiperazine-2-carboxylates and 1,4-diazepane-2,5-diones from methyl 2-chloro-2-cyclopropylideneacetate.
Limbach M1, Korotkov VS, Es-Sayed M, de Meijere A. Org Biomol Chem. 2008 Oct 21;6(20):3816-22. doi: 10.1039/b809174a. Epub 2008 Aug 13.
The 2-spirocyclopropanated methyl 5-oxopiperazine-2-carboxylate and the 3-spirocyclopropanated 6-chloro-1,4-diazepane-2,5-dione could both be prepared at choice in 93 and 88% yield, respectively, from methyl 2-chloro-2-cyclopropylideneacetate () in a sequence of Michael addition of 3-benzyloxypropylamine, peptide coupling with N-Boc-glycine, Boc-group removal and cyclization. Transformation of the benzyloxypropyl side chain, peptide coupling with N-Boc-(S)-asparagine, deprotection and repeated cyclization led to the octahydro[2H]pyrazino[1,2-a]pyrazinetrione scaffold containing a rigidified mimic of a tripeptide with a DGR motif. The overall yield of after deprotection of (a total of 13 steps in 8 distinct operations) was 30%.
3.Efficient construction of PET/fluorescence probe based on sarcophagine cage: an opportunity to integrate diagnosis with treatment.
Liu S1, Li D, Huang CW, Yap LP, Park R, Shan H, Li Z, Conti PS. Mol Imaging Biol. 2012 Dec;14(6):718-24. doi: 10.1007/s11307-012-0557-z.
PURPOSE: Due to the shortage of established platforms/methods for multimodality probe construction, in this study, we developed a heterofunctional chelator, BaAn(Boc)Sar, from sarcophagine cage as a general platform for dual-modality probe construction.
4.Application of carbodiimide mediated Lossen rearrangement for the synthesis of alpha-ureidopeptides and peptidyl ureas employing N-urethane alpha-amino/peptidyl hydroxamic acids.
Narendra N1, Chennakrishnareddy G, Sureshbabu VV. Org Biomol Chem. 2009 Sep 7;7(17):3520-6. doi: 10.1039/b905790k. Epub 2009 Jul 7.
Application of the Lossen rearrangement to the synthesis of N-urethane protected alpha-peptidyl ureas and ureidopeptides is reported. The carbodiimide mediated rearrangement of N-Boc/Z/Fmoc protected alpha-amino/peptide hydroxamic acids into isocyanates and coupling of the latter with the amino acid esters/peptide esters have been accomplished in a single-pot to obtain good yields of urea products. Synthesis of the ureidoalanine derivatives via the hydroxamate derivatives of N-protected aspartic acid has also been carried out using the same procedure.
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