59156-70-6

Usage

Uses

Used in Bioconjugation:
Di(N-succinimidyl) adipate is used as a crosslinking agent for bioconjugation, specifically for the covalent attachment of proteins, oligonucleotides, and other amine-containing molecules. This allows for the formation of stable amide bonds between the NHS ester groups and the primary amines, facilitating the creation of conjugates for various applications.
Used in Research and Diagnostics:
In the field of research and diagnostics, Di(N-succinimidyl) adipate is employed as a reagent for the development of immunoassays, enzyme-linked immunosorbent assays (ELISA), and other detection methods. Its ability to form stable bonds with amine-containing molecules makes it a valuable tool for the production of probes, sensors, and diagnostic kits.
Used in Drug Development:
Di(N-succinimidyl) adipate is utilized in the pharmaceutical industry for the synthesis of drug conjugates and the development of targeted drug delivery systems. Its crosslinking properties enable the attachment of therapeutic agents to specific carriers or targeting molecules, enhancing the drug's efficacy and selectivity.
Used in Materials Science:
In materials science, Di(N-succinimidyl) adipate is used as a coupling agent to modify the surface properties of various materials, such as polymers and nanoparticles. This allows for the creation of functionalized materials with specific binding properties, which can be applied in areas like sensors, catalysts, and biocompatible coatings.

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 124-04-9 Adipic acid 
• 123-56-8 Succinimide 
• 111-50-2 Adipic acid dichloride 

Downstream Products

• 50327-22-5 C₅₃H₈₆N₈O₁₆Sn 
• 1446417-14-6 (R)-2-(6-(((R)-1-carboxy-2-(tritylthio)ethyl)amino)-6-oxohexanamido)-3-(tritylthio)propanoic acid 

Relevant academic research and scientific papers

Chemical cross-linking and high-performance Fourier transform ion cyclotron resonance mass spectrometry for protein interaction analysis: Application to a calmodulin/target peptide complex

Chemical cross-linking has proved successful in combination with mass spectrometry as a tool for low-resolution structure determination of proteins. The integration of chemical cross-linking with Fourier transform ion cyclotron resonance (FTICR) mass spectrometry to determine protein interfaces was tested on the calcium-dependent complex between calmodulin (CaM) and a 26-amino acid peptide derived from the skeletal muscle myosin light chain kinase (M13). Different amine-reactive, homobifunctional cross-linkers and a "zero-length" cross-linker were employed. The covalently attached complexes were separated from nonreacted proteins by one-dimensional gel electrophoresis, and the bands of interest were excised and in-gel digested with trypsin. Digestion of the cross-linked complexes resulted in complicated peptide mixtures, which were analyzed by nano-HPLC/nano-ESI-FTICR mass spectrometry. The distance constraints obtained by chemical cross-linking were in agreement with the published NMR structure of the CaM/M13 complex, pointing to residues Lys-18 and Lys-19 of M13 being cross-linked with the central α-helix of CaM. Thus, the integrated approach described herein has proven to be an efficient tool for mapping the topology of the CaM/M13 complex. As such it is applicable as a general strategy for the investigation of the spatial organization of protein complexes and complements existing techniques, such as X-ray crystallography and NMR spectroscopy.

Synthesis and structure of bis(2,5-Dioxopyrrolidin-1-yl)adipate

bis(2,5-Dioxopyrrolidin-1-yl)adipate was prepared from adipate. Its structure was determined by single crystal X-ray diffraction analysis. The crystals are monoclinic space group P21/c with a = 5.2972(3), b = 7.5196(5), c = 19.2660(13) ?, α = 90.00, β = 99.776(6), γ = 90.00°, V = 756.28(8) ?3, Z = 2, F(000) = 356.0, Dc = 1.494 g/cm3, μ = 1.070 mm-1, the final R = 0.0511 and wR = 0.1135. A total of 2484 reflections were collected, of which 1342 were independent (Rint = 0.0255).

Modification of bovine serum albumin with aminophenylboronic acid as glycan sensor based on surface plasmon resonance and isothermal titration calorimetry

Aminophenylboronic acid (ABA) modified bovine serum albumin (BSA) was prepared as neolectin and its interactions with oligosaccharides and glycopolymer were studied by surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC). The conjuga

Polypeptide-engineered physical hydrogels designed from the coiled-coil region of cartilage oligomeric matrix protein for three-dimensional cell culture

Photo-cross-linkable physical hydrogels based on the coiled-coil region of the cartilage oligomeric matrix protein and polyethylene glycol diacrylate were designed and synthesized to mimic the natural extracellular matrix for three-dimensional cell culture. The engineered polypeptides (Pcys and RGDPcys) were modified with polyethylene glycol diacrylate to form photo-cross-linkable multifunctional macromers via the Michael-type addition reaction between the cysteine residues and acrylates. Gel formation was confirmed by rheological measurements. The swelling ratio and stability of 10% w/v RGDP-PEG-acrylate 6k hydrogel were 38% and 15 days, respectively. Spreading and migration of encapsulated fibroblast cells were observed in these physical hydrogels, while round cells were observed in a covalent control hydrogel. In addition, rapid self-healing of these physical hydrogels can provide a flexible way to build tissue by self-assembly and bottom-up approach. The results demonstrate that such physical hydrogels are expected to have great potential applications in tissue engineering.

Novel bivalent inhibitors with sub-nanomolar affinities towards human glyoxalase i

The zinc metalloenzyme glyoxalase I (GlxI) catalyzes the glutathione-dependent inactivation of cytotoxic methylglyoxal. Two competitive bivalent GlxI inhibitors, polyBHG2-62 (Ki = 1.0 nM) and polyBHG2-54 (Ki = 0.3 nM), were synthesiz

Conjugates of Aminopenicillins with Proteins: Synthesis, Immunogenic Properties, and Binding to the β-Lactam Receptor and Antibodies

Abstract: A new approach to aminopenicillin modification and conjugation with proteins was developed using di-N-hydroxysuccinimide esters of dicarboxylic acids as crosslinkers. Acylation of ampicillin (Amp) and amoxicillin (Amox) with di-N-hydroxysuccinimide esters of adipic or terephthalic acids was carried out in an organic solvent. Subsequent conjugation of the resulting aminopenicillin derivatives with proteins was done in an aqueous medium at pH 8.3 to produce immunogenic and enzymatic conjugates of Amp and Amox. The β-lactam cycle of Amp was shown to remain intact after chemical modification and synthesis of linker conjugates. An immunogenic Amp–thyroglobulin conjugate containing an aromatic linker was used for long-term immunization of rabbits, and polyclonal antibodies thus obtained were found to bind Amp, Amox, and penicillin G with extremely high sensitivity. Amp and Amox conjugates with horseradish peroxidase (HRP) were synthesized and characterized in a competitive protein-binding (receptor) assay and a direct competitive enzyme-linked immunosorbent assay (ELISA). Of the model immunoassay systems tested, the best characteristics were observed for heterologous direct ELISA with polyclonal antibodies and the Amp–HRP conjugate that contained an adipic acid fragment as a linker: the Amp sensitivity was 0.03 ng/mL and IC50 = 0.20 ng/mL.

DIPEPTIDE MIMETICS OF NGF AND BDNF NEUROTROPHINS

The invention relates to compounds having either agonist or antagonist activities for the neurotrophins NGF and BDNF and represented by monomeric or dimeric substituted dipeptides that are analogs of the exposed portions of loop 1 or loop 4 regions of these neurotrophins near or at a beta-turn of the respective loop. N-acylated substituents of these dipeptides are biostereoisomers of the amino acid residues preceding these dipeptide sequences in the neurotrophin primary structure. The dimeric structure is produced advantageously by using hexatnethylenediaanine to which dipeptides are attached via their carboxyl groups. The claimed compounds displayed neuroprotective and differentiation-inducing activities in cellular models and enhanced the amount of phosphorylated tyrosine kinase A and the heat shock proteins Hsp32 and Hsp70 in the concentration range of 10 -9 to 10 -5 M. They also displayed neuroprotective, anti-parkinsonian, anti-stroke, anti-ischemic, anti-depressant and anti-amnestic activities in animal models and were active in experimental models of Alzheimer's disease. These in vivo effects of the claimed compounds are displayed in the dose range of 0.01 to 10 mg/kg when administered intraperitoneally.

COMPOUNDS AND THERAPEUTIC USES THEREOF

The invention relates to novel compounds with the ability to link an immune response to a defined therapeutic target, to the use of said compounds in treating cancer and a disease or disorder mediated and/or caused by an infective agent, to compositions containing said compounds, processes for their preparation and to novel intermediates used in said process.

MODIFIED THERAPEUTIC AGENTS AND COMPOSITIONS THEREOF

Methods and compositions are provided for extending the half-life of a therapeutic agent. A modified therapeutic agent (mTA) comprises a therapeutic agent, a staple, and a half-life extending molecule. The mTAs disclosed herein may be used to treat a disease or a condition in a subject in need thereof.

Preparation and properties of gelatin films incorporated with N-hydroxysuccinimide-activated end-bit binary acid

A series of novel cross-linkers, N-hydroxysuccinimide (NHS)-activated end-bit binary acid (NHS-C4, C5, C6, C8, C10, C14), were synthesised to modify gelatin films and the crosslinking effects were compared. Homogeneous films with the exception of the film crosslinked by NHS-C14 were observed and the thickness was measured using a scanning electron microscope. The section feature influenced by different film-treatment conditions was also recorded. The differential scanning calorimetry results indicated higher thermal stability. The water contact angles confirmed enhanced hydrophobicity. NHS-C6, which was used as a probe crosslinker, exhibited the best crosslinking effect that the content of the free -NH2 achieved was the lowest out of all the crosslinkers. The biodegradation results of gelatin films modified by NHS-C6 exhibited better degradation-resistance and excellent stability. In addition, the optimal experimental conditions were 45°C for 12 h when [NHS-C6]/[-NH2] = 2.5.