Name: 4-Maleimidobutyric acid
Brand: BOC Sciences
Rating: 5 (1 reviews)

Synonyms

MBA; 2,5-Dihydro-2,5-dioxo-1H-pyrrole-1-butanoic Acid; N-(3-Carboxypropyl)maleimide; 1H-Pyrrole-1-butanoic acid, 2,5-dihydro-2,5-dioxo-; Maleimide-(CH2)3-COOH; 4-(2,5-dioxo-2H-pyrrol-1(5H)-yl)butanoic acid; 4-MaleimidobutyricAcid(GMBA); SCHEMBL155346; 2,5-Dioxo-3-pyrroline-1-butyric acid; γ-Maleimidobutyric acid; 4-Maleimidobutanoic acid; N-Maleoyl-4-aminobutyric acid; N-Maleoyl-GABA

IUPAC Name

4-(2,5-dioxopyrrol-1-yl)butanoic acid

Canonical SMILES

C1=CC(=O)N(C1=O)CCCC(=O)O

InChI

InChI=1S/C8H9NO4/c10-6-3-4-7(11)9(6)5-1-2-8(12)13/h3-4H,1-2,5H2,(H,12,13)

InChIKey

NCPQROHLJFARLL-UHFFFAOYSA-N

Density

1.395±0.06 g/cm<sup>3</sup> (Predicted)

Solubility

Slightly soluble in Chloroform, Ethyl Acetate; Very slightly soluble in Methanol

Melting Point

95-98 °C

Appearance

White powder

Shipping

Room temperature in continental US; may vary elsewhere.

Storage

2-8 °C

Signal Word

Warning

Boiling Point

400.1±28.0 °C (Predicted)

4-Maleimidobutyric acid, a versatile chemical compound used in diverse research and industrial settings, finds applications across various domains. Here are four key applications highlighted with elevated perplexity and burstiness:

Bioconjugation: A cornerstone of modern biochemistry, 4-Maleimidobutyric acid plays a vital role in conjugating proteins, peptides, and antibodies with other molecules like drugs or fluorescent labels. Its maleimide group exhibits selective reactivity with thiol groups, enabling precise coupling under gentle conditions. This method is crucial for crafting targeted therapeutics and diagnostic tools tailored to specific molecular interactions.

Drug Delivery: Positioned at the forefront of pharmaceutical innovation, 4-Maleimidobutyric acid contributes to the design of advanced drug delivery systems that ensure the controlled and targeted release of therapeutic agents. By linking drugs to polymeric carriers or nanoparticles, it enhances drug stability and specificity, ultimately improving treatment efficacy while minimizing undesirable side effects. This approach represents a paradigm shift in drug delivery strategies.

Surface Modifications: Delving into the realm of biomaterials, 4-Maleimidobutyric acid is instrumental in enhancing the biocompatibility and functionality of material surfaces. By grafting bioactive molecules, such as adhesion-promoting peptides or antifouling agents, it enhances material-biological interactions crucial for developing cutting-edge medical implants and biosensors. This application showcases the synergy between chemistry and biomedicine in creating advanced biofunctional materials.

Enzyme Immobilization: At the intersection of biocatalysis and industrial applications, 4-Maleimidobutyric acid facilitates the immobilization of enzymes on diverse supports, elevating their stability and reusability in enzymatic reactions. Through covalent bonding between the maleimide group and enzyme thiol groups, enzymes are firmly anchored onto carrier materials, ensuring consistent performance over multiple cycles. This technique is pivotal for industries reliant on enzymatic processes, underscoring the importance of enzyme stability in enhancing productivity and efficiency.

1. Preparation of peptide-conjugated quantum dots for tumor vasculature-targeted imaging

Weibo Cai, Xiaoyuan Chen Nat Protoc. 2008;3(1):89-96. doi: 10.1038/nprot.2007.478.

To take full advantage of the unique optical properties of quantum dots (QDs) and expedite future near-infrared fluorescence (NIRF) imaging applications, QDs need to be effectively, specifically and reliably directed to a specific organ or disease site after systemic administration. Recently, we reported the use of peptide-conjugated QDs for non-invasive NIRF imaging of tumor vasculature markers in small animal models. In this protocol, we describe the detailed procedure for the preparation of such peptide-conjugated QDs using commercially available PEG-coated QDs and arginine-glycine-aspartic acid (RGD) peptides. Conjugation of the thiolated RGD peptide to the QDs was achieved through a heterobifunctional linker, 4-maleimidobutyric acid N-succinimidyl ester. Competitive cell binding assay, using (125)I-echistatin as the radioligand, and live cell staining were carried out to confirm the successful attachment of the RGD peptides to the QD surface before in vivo imaging of tumor-bearing mice. In general, QD conjugation and in vitro validation of the peptide-conjugated QDs can be accomplished within 1-2 d; in vivo imaging will take another 1-2 d depending on the experimental design.

2. Paclitaxel conjugation with the analog of the gonadotropin-releasing hormone as a targeting moiety

Marie Pribylova, Marcela Dvorakova, Veronika Hanusova, Ingrid Nemethova, Lenka Skalova, Tomas Vanek Int J Pharm. 2011 Aug 30;415(1-2):175-80. doi: 10.1016/j.ijpharm.2011.05.072. Epub 2011 Jun 12.

A new targeted conjugates in which paclitaxel was used as a cytostatic compound and an analog of the gonadotropin-releasing hormone (GnRH) as a targeting moiety were synthesized. The molecule of the peptide hormone GnRH was modified to allow its connection to paclitaxel via spacer. The conjugates were prepared as prodrugs using 2'-hydroxyl group of paclitaxel. 4-Maleimidobutyric acid and chloroacetic acid served as spacers. The structures of the prepared derivatives were analysed by NMR and HR-MS. The conjugates MP264 and MP265 were chosen and their antiproliferative effect was tested in the breast cancer cell line MCF-7 using the MTT test of cell viability and neutral red uptake test. In MCF-7 cells, conjugate MP265 showed higher antiproliferative effect than paclitaxel alone. Receptor saturation tests showed that the unconjugated peptide analog of GnRH decreased efficacy of conjugate MP265 in concentration- and time-dependent manner. In conclusion, the paclitaxel conjugate with the analog of GnRH exhibited targeted antiproliferative effect for which its further testing will be implemented.

3. Interfacial recognition of human prostate-specific antigen by immobilized monoclonal antibody: effects of solution conditions and surface chemistry

Xiubo Zhao, Fang Pan, Luis Garcia-Gancedo, Andrew J Flewitt, Gregory M Ashley, Jikui Luo, Jian R Lu J R Soc Interface. 2012 Oct 7;9(75):2457-67. doi: 10.1098/rsif.2012.0148. Epub 2012 May 2.

The specific recognition between monoclonal antibody (anti-human prostate-specific antigen, anti-hPSA) and its antigen (human prostate-specific antigen, hPSA) has promising applications in prostate cancer diagnostics and other biosensor applications. However, because of steric constraints associated with interfacial packing and molecular orientations, the binding efficiency is often very low. In this study, spectroscopic ellipsometry and neutron reflection have been used to investigate how solution pH, salt concentration and surface chemistry affect antibody adsorption and subsequent antigen binding. The adsorbed amount of antibody was found to vary with pH and the maximum adsorption occurred between pH 5 and 6, close to the isoelectric point of the antibody. By contrast, the highest antigen binding efficiency occurred close to the neutral pH. Increasing the ionic strength reduced antibody adsorbed amount at the silica-water interface but had little effect on antigen binding. Further studies of antibody adsorption on hydrophobic C8 (octyltrimethoxysilane) surface and chemical attachment of antibody on (3-mercaptopropyl)trimethoxysilane/4-maleimidobutyric acid N-hydroxysuccinimide ester-modified surface have also been undertaken. It was found that on all surfaces studied, the antibody predominantly adopted the 'flat on' orientation, and antigen-binding capabilities were comparable. The results indicate that antibody immobilization via appropriate physical adsorption can replace elaborate interfacial molecular engineering involving complex covalent attachments.