4-Maleimidobutyric acid
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4-Maleimidobutyric acid

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4-Maleimidobutyric Acid is a short crosslinking reagent.

Category
Peptide Synthesis Reagents
Catalog number
BAT-006297
CAS number
57078-98-5
Molecular Formula
C8H9NO4
Molecular Weight
183.16
4-Maleimidobutyric acid
IUPAC Name
4-(2,5-dioxopyrrol-1-yl)butanoic acid
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
Appearance
White powder
Purity
98 % (HPLC)
Density
1.395±0.06 g/cm3 (Predicted)
Melting Point
95-98 ℃
Boiling Point
400.1±28.0 ℃ (Predicted)
Storage
2-8 ℃
Solubility
Slightly soluble in Chloroform, Ethyl Acetate; Very slightly soluble in Methanol
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)
InChI Key
NCPQROHLJFARLL-UHFFFAOYSA-N
Canonical SMILES
C1=CC(=O)N(C1=O)CCCC(=O)O
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.
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