64191-06-6

Usage

Uses

Used in Research and Diagnostic Applications:
4-N-Maleimidobenzoic acid-NHS is used as a bioconjugation agent for the covalent linkage of proteins or peptides to other molecules. Its high specificity and reactivity enable the formation of stable conjugates, which are essential for various research and diagnostic purposes, such as the development of biosensors, immunoassays, and enzyme-linked immunosorbent assays (ELISAs).
Used in Antibody Labeling:
In the field of immunology, 4-N-Maleimidobenzoic acid-NHS is employed as a labeling agent for antibodies. 4-N-Maleimidobenzoic acid-NHS's ability to form stable thioether bonds with thiol-containing antibodies allows for the attachment of fluorescent dyes, biotin, or other reporter groups, enabling the detection and quantification of specific antigens in various assays.
Used in Protein Immobilization:
4-N-Maleimidobenzoic acid-NHS is utilized as a protein immobilization agent in the development of biosensors and affinity chromatography systems. 4-N-Maleimidobenzoic acid-NHS's reactivity with thiol groups allows for the covalent attachment of proteins to solid supports, enhancing their stability and enabling their use in various analytical and diagnostic applications.
Used in Drug Delivery Systems:
In the pharmaceutical industry, 4-N-Maleimidobenzoic acid-NHS is used as a component in the design of targeted drug delivery systems. 4-N-Maleimidobenzoic acid-NHS's ability to form stable conjugates with proteins or peptides enables the development of drug carriers with specific targeting capabilities, improving the therapeutic efficacy and reducing side effects of various treatments.

Upstream product

• 108-31-6 maleic anhydride 
• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 150-13-0 4-amino-benzoic acid 
• 17057-04-4 N-(4-carboxyphenyl)maleimide 
• 5672-89-9 N-trifluoroacetoxy succinimide 
• 5432-04-2 N-(4-carboxyphenyl)maleamic acid 

Relevant academic research and scientific papers

Synthesis, characterization, and targeted chemotherapy of SCT200-linker-monomethyl auristatin E conjugates

Antibody-drug conjugates (ADCs) are currently among the most successful and important strategies for treating patients with solid tumors. ADCs are composed of a monoclonal antibody and warhead, which are conjugated via a linker. Currently, monomethyl auristatin E (MMAE) is the most widely applied warhead in the development of ADCs. However, MMAE-based ADCs are generally constructed using the MC-VC-PABC linker, and this design has limited structural diversity and some disadvantages. Accordingly, in this study, we generated three types of novel linker-MMAE (with alterations in the spacer, catabolizing area, and self-immolative compared with MC-VC-PABC-MMAE) in ADCs, termed SCT200-linker-MMAE conjugates, and then evaluated the linker-drug plasma stability and the rate of drug release by cathepsin B. The binding ability, internalization rates, and efficacy of all SCT200-linker-MMAE ADCs were systematically studied, and the expression of apoptosis-associated proteins and the therapeutic efficacies of SCT200-M-2, -C-2, and -C-4 were evaluated. The results showed that the activities of some of these ADCs were increased for epidermal growth factor receptor-positive tumors. Moreover, the novel linkers designed in this study can be linked with other antibodies to treat other types of cancer. Overall, these findings provide important insights into the application of SCT200-based linkers in ADCs.

In situ formation of N-trifluoroacetoxy succinimide (TFA-NHS): One-pot formation of succinimidyl esters, N-trifluoroacetyl amino acid succinimidyl esters, and N-maleoyl amino acid succinimidyl esters

A method for the in situ formation of N-trifluoroacetoxy succinimide (TFA-NHS) and its application in the formation of succinimidyl esters is presented. The developed method provides N-trifluoroacetyl and N-maleoyl amino acid succinimidyl esters from a variety of amino acids using a one-pot, high-yielding protocol. Investigations into the formation of an N-maleoyl amino acid succinimidyl ester supported the proposal of a revised reaction mechanism, and contributed to the optimization of the reaction conditions.

Practical synthesis of maleimides and coumarin-linked probes for protein and antibody labelling via reduction of native disulfides

The cellular tracking, detection and sensing of protein or antibody movement are important aspects to advance our understanding of biomolecular interactions and activity. Antibodies modified with fluorescent dyes are also valuable tools, especially in immunology research. We describe here a proof-of-principle study of a new water-soluble coumarin probe with a maleimide thiol-reacting unit to fluorescently tag biomolecules. Highlights include: (1) a convenient water-based preparation of N-substituted maleimides, (2) a one-pot preparation of activated maleimido-esters, and (3) a bio-conjugation protocol for the selenol-promoted reduction of native disulfide bonds and the 'site-specific' labelling of antibodies with no significant loss of activity.

Convenient preparation of N-maleoyl amino acid succinimido esters using N-trifluoroacetoxysuccinimide

One-pot cyclization and esterification of readily available maleamic acid derivatives using N-trifluoroacetoxysuccinimide provide a convenient and cost-effective route to a variety of useful N-maleoyl amino acid N-hydroxysuccinimido esters. Copyright Taylor & Francis Group, LLC.

Facile synthesis of reagents containing a terminal maleimido ligand linked to an active ester

Condensation of ω-amino acids with maleic anhydride to yield maleamino acids and subsequent esterification with N-hydroxysuccinimide, 3,4-dihydro-3-hydroxy-4-oxo-1,2,3-benzotriazine, or pentafluorophenol to give the corresponding esters in a one pot procedure are described. The reagents can be isolated and purified without chromatography in 7-55% yields.

Synthesis of N-Maleoyl-aminoacids and -peptides

N-Maleoyl-aminoacid-N'-hydroxysuccinimidesters 3 or N-maleoyl-aminobenzoic acids 5 are synthsized from N-maleyl-aminoacids 1 on different ways.N-maleoyl-aminobenzoic-4-nirophenyl-, -2-nitro-phenyl- or 2,4-dinitro-phenylesters 6, 7 and 8 will be obtained from 1 or 5. o-Mercaptoaniline, thiourea or cysteine react with 5 to benzothiazines 9, thiazolidines 10 and 1,4-thiazines 11.From 5 the peptides 12 are yielded.The pentapeptide 13 are formed from 12 by addition of glutathione.

Preparation and Characterization of Hetero-bifunctional Cross-linking Reagents for Protein Modifications

Ten aromatic and aliphatic cross-linking reagents of hetero-bifunctional type were synthesized as part of a search for useful reagents of this type.All of the reagents possess two selectively reactive groups a maleimide group which can combine with a thiol group via its double bond and an N-Hydroxysuccinimidyl ester (one of the most hydrophilic active esters), which can react with an ammmine group.It was found that the active esters of the reagents tested were mostly more reactive with lysine than with leucine, and acylated amino acids more rapidly at pH 8.0 than at pH 7.0.It was also found that the stability of the maleimide group in the compounds tested depends largely upon the pH of the buffer used.The most stable pH was 5.0-6.0.To use one of the present compounds as a cross-linker, the crystalline reagent should be dissolved in tetrahydrofuran of dioxane and the solution used for cross-linking.The acylation step should be carried out first with thiol addition to the maleimide group as the second step.The optimum pH of the buffer used for the first step is slightly basic.The reaction time should be limited to less than 1 hr.When the first step is over, the pH of the reaction mixture should be changed to 5.0-6.0.Keywords---cross-linker; hetero-bifunctional reagent; reactivity of N-hydroxy-succinimidyl ester; stability of maleimide residue; N-(maleimidobenzoyloxy)succinimide derivative; N-(maleimidoalkyloxy)succinimide derivative