80366-85-4

Basic information

• Product Name: t-Boc-aminooxyacetic Acid N-Hydroxysuccinimide Ester
• Synonyms: 2-[[[(1,1-DiMethylethoxy)carbonyl]aMino]oxy]acetic Acid 2,5-Dioxo-1-pyrrolidinyl Ester;N-Bocaminooxy-aceticacid2,5-dioxo-pyrrolidin-1-ylester;Boc-Aoa-NHS;Boc-Aoa-OSu;N-Boc-aminooxyacetic acidN-hydroxysuccinimide ester≥ 98% (Assay);t-Boc-aminooxyacetic Acid N-Hydroxysuccinimide Ester ;[2-[(2,5-Dioxo-1-pyrrolidinyl)oxy]-2-oxoethoxy]carbaMic Acid 1,1-DiMethylethyl Ester;N-Succinimidyl [(tert-Butoxycarbonyl)aminooxy]acetate
• CAS NO: 80366-85-4
• Molecular Formula: C₁₁H₁₆N₂O₇
• Molecular Weight: 288.25394
• Product Categories: Cross Linking Reagents;Heterocycles
• Mol File: 80366-85-4.mol

Chemical Properties

• Melting Point: 108-110°C
• Appearance: /
• Storage Temp.: Hygroscopic, Refrigerator, Under Inert Atmosphere
• Solubility: Chloroform (Slightly), DMSO (Slightly), Ethyl Acetate (Slightly)
• CAS DataBase Reference: t-Boc-aminooxyacetic Acid N-Hydroxysuccinimide Ester(CAS DataBase Reference)
• NIST Chemistry Reference: t-Boc-aminooxyacetic Acid N-Hydroxysuccinimide Ester(80366-85-4)
• EPA Substance Registry System: t-Boc-aminooxyacetic Acid N-Hydroxysuccinimide Ester(80366-85-4)

Safety Data

• Hazardous Substances Data: 80366-85-4(Hazardous Substances Data)

Usage

Uses

Used in Bioconjugation Applications:
t-Boc-aminooxyacetic Acid N-Hydroxysuccinimide Ester is used as a heterobifunctional linker for the facile access to bioconjugates. Its unique chemical properties allow for the efficient and specific attachment of various biomolecules, such as peptides, proteins, and other functional groups, enabling the development of novel bioconjugates with diverse applications in research, diagnostics, and therapeutics.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, t-Boc-aminooxyacetic Acid N-Hydroxysuccinimide Ester is used as a key intermediate in the synthesis of drug conjugates. Its ability to form stable and functional bioconjugates allows for the development of targeted drug delivery systems, improving the efficacy and reducing the side effects of various therapeutic agents.
Used in Research and Development:
t-Boc-aminooxyacetic Acid N-Hydroxysuccinimide Ester is also used in research and development for the creation of novel bioconjugates with potential applications in various fields, such as diagnostics, imaging, and therapeutics. Its versatility and ease of use make it an attractive option for scientists and researchers working on the development of new bioconjugate-based technologies.

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 42989-85-5 [({[(2-methyl-2-propanyl)oxy]carbonyl}amino)oxy]acetic acid 
• 24424-99-5 di-tert-butyl dicarbonate 

Downstream Products

• 679406-28-1 C₁₉H₂₄F₃N₅O₆ 
• 1180490-95-2 C₂₉H₂₉N₅O₄ 

Relevant articles and documents

Overcoming drug resistance by cell-penetrating peptide-mediated delivery of a doxorubicin dimer with high DNA-binding affinity

We describe the synthesis and characterization of a novel bioconjugate, consisting of an octaarginine cell-penetrating peptide and a highly DNA-affine doxorubicin dimer. The linkage between the two components is composed of a cleavable disulfide bond, which enables the efficient intracellular delivery of the cytotoxic payload within the reductive environment of the cytosol, mediated through glutathione. To determine the DNA-binding affinity of the dimeric drug molecule, microscale thermophoresis was applied. This is the first utilization of this method to assess the binding interactions of an anthracycline drug with nucleic acids. The cytotoxic effect of the peptide-drug conjugate, studied with drug-sensitive and doxorubicin-resistant cancer cells, demonstrates that the bioconjugate can successfully overcome drug resistance in neuroblastoma cells.

Molecular imaging of cancer cells using a bacteriophage-based 129Xe NMR biosensor

NMR imaging: Filamentous fd bacteriophage expressing antibodies recognizing the epidermal growth factor receptor (EGFR) were modified to incorporate cage-like xenon-binding molecules (CryA). The resulting contrast agent was shown to bind to an EGFR-positive cell line and detected by hyperpolarized 129Xe NMR spectroscopy using chemical exchange saturation transfer (hyperCEST, see picture). Copyright

An amino acid-based heterofunctional cross-linking reagent

We describe the synthesis and characterization of a new lysine-based heterofunctional cross-linking reagent. It carries two readily available aminooxy functionalities and an activated and protected thiol group that is capable of generating reducible disulfides, the former enable bioorthogonal modification of ketones and aldehydes by the formation of an oxime bond. The efficacy of the linker was proven by coupling two doxorubicin molecules to the functionalized amino acid core and the subsequent bioconjugation of this drug conjugate with a thiolated antibody. Graphical Abstract: [Figure not available: see fulltext.]

Multivalency: Key Feature in Overcoming Drug Resistance with a Cleavable Cell-Penetrating Peptide-Doxorubicin Conjugate

Multivalency is often used in biological systems, to increase affinity and specificity through avidity. This inspired us to prepare a synthetic bioconjugate that mimics natural multivalent systems. It is composed of doxorubicin and two octaarginine cell-penetrating peptides, to strengthen the electrostatic interactions between the negatively charged glycosaminoglycans of the plasma membrane and the guanidinium groups of the arginine residues. The multivalent conjugate has improved cellular uptake and cytotoxicity, compared to a peptide-drug conjugate with only one polyarginine and as a result it can overcome drug resistance in Kelly-ADR cells. The synthetic approach and the multivalent structure reported here can be used further as model systems, to gain insight into the biological interaction of cell-penetrating peptides with artificial membranes or for the preparation of more complex multimers.

Ethoxyethylidene protecting group prevents N-overacylation in aminooxy peptide synthesis

We report herein an improved synthetic route for the preparation of homogenous aminooxy peptides suitable for oxime ligation. Aminooxyacetic acid (Aoa) was protected with 1-ethoxyethylidene group (Eei) then incorporated either using PyBOP or as N-hydroxysuccinimidyl ester at N-terminal end or at a lysine side chain into model peptides in solution and on solid support. Due to the Eei protecting group, these new reagents prevent the N-overacylation side reaction in comparison with Boc-Aoa derivatives. Subsequent deprotection under mild acidic conditions gave the corresponding pure aminooxylated peptides.

Synthesis and biological evaluation of a siderophore-virginiamycin conjugate

Condensation of Virginiamycin S1 (1) with aminooxyacetic acid afforded oxime 9. EDC/HOAt-mediated coupling of 9 to the N-terminus of the tripeptide of N5-hydroxy-N5-acetyl-L-ornithine, the common iron chelator in most hydr

One-pot: N -glycosylation remodeling of IgG with non-natural sialylglycopeptides enables glycosite-specific and dual-payload antibody-drug conjugates

Chemoenzymatic transglycosylation catalyzed by endo-S mutants is a powerful tool for in vitro glycoengineering of therapeutic antibodies. In this paper, we report a one-pot chemoenzymatic synthesis of glycoengineered Herceptin using an egg-yolk sialylglycopeptide (SGP) substrate. Combining this one-pot strategy with novel non-natural SGP derivatives carrying azido or alkyne tags, glycosite-specific conjugation was enabled for the development of new antibody-drug conjugates (ADCs). The site-specific ADCs and semi-site-specific dual-drug ADCs were successfully achieved and characterized with SDS-PAGE, intact antibody or ADC mass spectrometry analysis, and PNGase-F digestion analysis. Cancer cell cytotoxicity assay revealed that small-molecule drug release of these ADCs relied on the cleavable Val-Cit linker fragment embedded in the structure. These results represent a new approach for glycosite-specific and dual-drug ADC design and rapid synthesis, and also provide the structural requirement for their biologic activities.

Orthogonal dual-modification of proteins for the engineering of multivalent protein scaffolds

To add new tools to the repertoire of protein-based multivalent scaffold design, we have developed a novel dual-labeling strategy for proteins that combines residue-specific incorporation of unnatural amino acids with chemical oxidative aldehyde formation at the N-terminus of a protein. Our approach relies on the selective introduction of two different functional moieties in a protein by mutually orthogonal copper-catalyzed azide-alkyne cycloaddition (CuAAC) and oxime ligation. This method was applied to the conjugation of biotin and β-linked galactose residues to yield an enzymatically active thermophilic lipase, which revealed specific binding to Erythrina cristagalli lectin by SPR binding studies.

Versatile and Efficient Site-Specific Protein Functionalization by Tubulin Tyrosine Ligase

A novel chemoenzymatic approach for simple and fast site-specific protein labeling is reported. Recombinant tubulin tyrosine ligase (TTL) was repurposed to attach various unnatural tyrosine derivatives as small bioorthogonal handles to proteins containing a short tubulin-derived recognition sequence (Tub-tag). This novel strategy enables a broad range of high-yielding and fast chemoselective C-terminal protein modifications on isolated proteins or in cell lysates for applications in biochemistry, cell biology, and beyond, as demonstrated by the site-specific labeling of nanobodies, GFP, and ubiquitin.

POLYMER ENHANCEMENT OF ENZYMATIC ACTIVITY

Provided herein are methods for enhancing enzymatic activity using certain polymers that may be optionally attached to an enzyme. The polymers may be thermally-responsive polymers, including poly N-isopropylacrylamide or poly N-isopropylmethacrylamide. The polymer may also be a copolymer with at least two different monomer residues. The monomer residues may have a structure of formula (I): wherein R1, RA and RB are as described herein. Examples of such monomer residues may include N-isopropylacrylamide (NIPAm) or N-isopropylmethacrylamide (NIPMa). The polymer may include additional monomer residues, such as aminooxy-bearing methacrylamide monomer residues that can be modified to vary the lower critical solution temperature (LCST) of the polymer.