Need Assistance?

US & Canada:
+
UK: +

FAQs

Resources

Our Highlights

GMP Grade Efficient workshop for GMP production.
Optimal Prices Buying products on this site guarantees the best price!
Commercial Batches Independent GMP manufacturing suites that handle commercial batches
Prompt Delivery Warehouses in multiple cities to ensure timely delivery
Flexible Quantity Quantities available from milligrams to ton

Application Area

Z-L-aspartic acid b-tert-butyl ester a-N-hydroxysuccinimide ester

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

Category

CBZ-Amino Acids

Catalog number

BAT-003327

CAS number

3338-32-7

Molecular Formula

C20H24N2O8

Molecular Weight

420.40

Z-L-aspartic acid b-tert-butyl ester a-N-hydroxysuccinimide ester

IUPAC Name

4-O-tert-butyl 1-O-(2,5-dioxopyrrolidin-1-yl) (2S)-2-(phenylmethoxycarbonylamino)butanedioate

Synonyms

Z-L-Asp(OtBu)-Osu; (S)-4-Tert-Butyl 1-(2,5-Dioxopyrrolidin-1-Yl) 2-(((Benzyloxy)Carbonyl)Amino)Succinate

Appearance

White to off-white powder

Purity

≥ 98% (HPLC)

Density

1.32 g/cm3

Melting Point

148-157 °C

Storage

Store at 2-8 °C

InChI

InChI=1S/C20H24N2O8/c1-20(2,3)29-17(25)11-14(18(26)30-22-15(23)9-10-16(22)24)21-19(27)28-12-13-7-5-4-6-8-13/h4-8,14H,9-12H2,1-3H3,(H,21,27)/t14-/m0/s1

InChI Key

JUMSBOKRGDETHL-AWEZNQCLSA-N

Canonical SMILES

CC(C)(C)OC(=O)CC(C(=O)ON1C(=O)CCC1=O)NC(=O)OCC2=CC=CC=C2

Z-L-aspartic acid β-tert-butyl ester α-N-hydroxysuccinimide ester (Z-Asp-OBu-t α-NHS ester) is a versatile compound extensively utilized in peptide synthesis and bioconjugation applications. Here are four key applications of Z-L-aspartic acid β-tert-butyl ester α-N-hydroxysuccinimide ester depicted with high perplexity and burstiness:

Peptide Synthesis: Playing a pivotal role in peptide synthesis, Z-As-As-OBu-t α-NHS ester facilitates the coupling of amino acids, enabling the formation of peptide chains with remarkable efficiency. Its hydroxysuccinimide ester group swiftly reacts with amine groups, establishing stable amide bonds crucial for the production of custom peptides used in diverse research and pharmaceutical settings. This reagent stands as a cornerstone for achieving high-yield peptide synthesis outcomes, advancing scientific endeavors.

Protein Labeling: Delving into protein labeling applications, this compound proves highly effective in labeling proteins through its reactive ester group capable of forging covalent bonds with lysine residues on proteins. Through the attachment of various labels, such as fluorescent dyes or biotin, researchers gain the ability to monitor and investigate protein interactions and localizations within biological systems. This approach, essential for immunoassays and cell imaging techniques, opens new avenues for understanding complex protein behaviors.

Surface Functionalization: In the realm of surface functionalization, Z-As-OBu-t α-NHS ester emerges as a key player, facilitating the modification of surfaces to suit specific applications. By attaching peptides or proteins to surfaces of nanoparticles, biosensors, or medical devices, it enhances their biocompatibility and functionality, laying the foundation for advanced diagnostic tools and targeted drug delivery systems.

Biomedical Research: Within the realm of biomedical research, Z-As-As-OBu-t α-NHS ester serves as a critical tool in crafting biomaterials endowed with specific functionalities through the conjugation of biologically active molecules. This versatile compound plays a crucial role in creating hydrogel matrices for tissue engineering or drug-loaded scaffolds for controlled release. These tailor-made materials hold immense potential in enhancing therapeutic outcomes and refining the design of biomedical devices.

1. Use of molecularly imprinted polymers in a biotransformation process

L Ye, O Ramström, R J Ansell, M O Månsson, K Mosbach Biotechnol Bioeng. 1999 Sep 20;64(6):650-5.

Molecularly imprinted polymers are highly stable and can be sterilised, making them ideal for use in biotransformation process. In this communication, we describe a novel application of molecularly imprinted polymers in an enzymatic reaction. The enzymatic condensation of Z-L-aspartic acid with L-phenylalanine methyl ester to give Z-L-Asp-L-Phe-OMe (Z-aspartame) was chosen as a model system to evaluate the applicability of using molecularly imprinted polymers to facilitate product formation. When the product-imprinted polymer is present, a considerable increase (40%) in product yield is obtained. Besides their use to enhance product yields, as demonstrated here, we suggest that imprinted polymers may also find use in the continuous removal of toxic compounds during biochemical reactions.

2. Synthesis of aspartame precursor: alpha-L-aspartyl-L-phenylalanine methyl ester in ethyl acetate using thermolysin entrapped in polyurethane

C P Yang, C S Su Biotechnol Bioeng. 1988 Aug 20;32(5):595-603. doi: 10.1002/bit.260320504.

Cross-linked polyurethane (PU) was prepared for entrapping thermolysin. Using the immobilized thermolysin (IT), Z-L-aspartic acid (ZA) was reacted with -Lphenylalanine methyl ester (L-PM) in water-saturated ethyl acetate to give only alpha-Z-L-aspartylL-phenylalanine methyl ester (alpha-ZAPM). Ninety-four percent conversion of alpha-ZAPM was obtained for 30 h of reaction at 40 degrees C when 46 mg of enzyme was entrapped. PU support prepared from polypropylene glycol (#2000) showed better properties than from polypropylene (#1000) and polyethylene (#1000). Addition of polyol could increase the gel fraction of PU. The IT PU-ll-G-3, prepared from 1/2 mole ratio of PPG (#2000)/glycerin, gave the highest gel fraction and best swelling, and 89.0% of residual activity was obtained after four times of reuse (72 h). The stability of immobilized thermolysin was good; the activity loss resulting from degradatin and leak of enzyme in each time of reuse were found only about 2%. The kinetics of immobilized thermolysin-catalyzed condensation reaction of ZA with L-PM in water-saturated ethyl acetate was found to be first order in L-PM and the Lineweaver-Burk plot of 1/V against 1/[ZA] yields a straight line, showing that the reaction involves consecutive reactions of ZA and L-PM with the immobilized enzyme and with the ZA-immobilized enzyme complex, with the second reaction being the rate determining step.

3. A new application of molecularly imprinted materials

L Ye, O Ramström, M O Månsson, K Mosbach J Mol Recognit. 1998 Winter;11(1-6):75-8. doi: 10.1002/(SICI)1099-1352(199812)11:1/63.0.CO;2-Q.

We have studied the possibility of shifting a thermodynamically unfavourable enzymatic equilibrium towards product formation via the addition of a highly specific adsorbent. The commercially interesting enzymatic condensation of Z-L-aspartic acid with L-phenylalanine methyl ester to the sweetener aspartame was chosen as the model system. Extremely stable and specific adsorbents for the product Z-L-Asp-L-Phe-OMe (Z-aspartame) were prepared using the emerging technique of molecular imprinting. A considerable increase (40%) in the yield of product was obtained when such adsorbents were present during the enzymatic reaction. The message of this investigation is that the use of such specific, sterilizable adsorbents should be considered for enzymatic processes to increase the yield. Finally, the direct isolation of a product formed by the retrieval of the adsorbents carrying the product can be envisaged, especially if the adsorbents are magnetic.