Name: GMBS
Brand: BOC Sciences
Rating: 5 (1 reviews)

Synonyms

4-Maleimidobutyric acid N-succinimidyl ester; N-(gamma-Maleimidobutyryloxy)succinimide; 4-Maleimidobutyric acid N-hydroxysuccinimide ester; 4-Maleimidobutyric acid n-succinimidyl ester; (GMBS);4-Maleimidobutyric acid NHS

IUPAC Name

(2,5-dioxopyrrolidin-1-yl) 4-(2,5-dioxopyrrol-1-yl)butanoate

Canonical SMILES

C1CC(=O)N(C1=O)OC(=O)CCCN2C(=O)C=CC2=O

InChI

InChI=1S/C12H12N2O6/c15-8-3-4-9(16)13(8)7-1-2-12(19)20-14-10(17)5-6-11(14)18/h3-4H,1-2,5-7H2

InChIKey

PVGATNRYUYNBHO-UHFFFAOYSA-N

Density

1.490±0.10 g/cm3 (Predicted)

Solubility

Slightly soluble in chloroform, methanol (heated)

Melting Point

123-129 °C

Flash Point

232.8±29.3 °C

Index Of Refraction

1.595

PSA

101.06000

Vapor Pressure

0.0±1.1 mmHg at 25°C

Appearance

Light Yellow to Off-white Solid

Shipping

Room temperature, or blue ice upon request.

Storage

-20 °C under inert atmosphere

Pictograms

Irritant

Signal Word

Warning

Boiling Point

461.3±47.0 °C (Predicted)

NCT Number	Condition Or Disease	Phase	Start Date	Sponsor	Status
NCT00294580	Malaria	Phase 4	2015-05-28	Imperial College London	Completed
NCT01660646	Tuberculosis	Not Applicable	2018-03-22	London School of Hygiene and Tropical Medicine	Completed
NCT01847872	Poliomyelitis	Phase 4	2018-03-22	London School of Hygiene and Tropical Medicine	Completed
NCT00944840	Malaria	Phase 3	2017-01-26	London School of Hygiene and Tropical Medicine	Completed
NCT04703608	Covid-19	Phase 3	2021-06-04	London School of Hygiene and Tropical Medicine	Recruiting

GMBS, also known as N-γ-Maleimidobutyryl-oxysuccinimide ester, stands out as a heterobifunctional crosslinker with widespread applications in bioscience research and development. Here are four key applications of GMBS:

Protein Crosslinking: A fundamental use of GMBS lies in linking proteins via their amine and thiol groups, leading to the formation of stable protein conjugates. This process is pivotal for investigating protein-protein interactions and constructing intricate macromolecular assemblies. By strategically crosslinking specific proteins, researchers can delve deep into interaction networks and unravel the multifaceted functions of proteins within biological systems.

Antibody Labeling: GMBS finds its place in antibody conjugation, facilitating the attachment of various labels like fluorescent dyes or enzymes to antibodies. This enables the creation of labeled antibodies, essential for applications in immunoassays, imaging, and diagnostics.

Drug Delivery Systems: Employing GMBS to crosslink drug molecules to carriers, such as nanoparticles or polymers, opens up avenues for targeted drug delivery. This innovative application plays a crucial role in enhancing the therapeutic index and minimizing drug side effects by directing them to specific tissues or cells.

1.Surface immobilization of neural adhesion molecule L1 for improving the biocompatibility of chronic neural probes: In vitro characterization.

Azemi E1, Stauffer WR, Gostock MS, Lagenaur CF, Cui XT. Acta Biomater. 2008 Sep;4(5):1208-17. doi: 10.1016/j.actbio.2008.02.028. Epub 2008 Mar 20.

Silicon-based implantable neural electrode arrays are known to experience failure during long-term recording, partially due to host tissue responses. Surface modification and immobilization of biomolecules may provide a means to improve their biocompatibility and integration within the host brain tissue. Previously, the laminin biomolecule or laminin fragments have been used to modify the neural probe's silicon surface to promote neuronal attachment and growth. Here we report the successful immobilization of the L1 biomolecule on a silicon surface. L1 is a neuronal adhesion molecule that can specifically promote neurite outgrowth and neuronal survival. Silane chemistry and the heterobifunctional coupling agent 4-maleimidobutyric acid N-hydroxysuccinimide ester (GMBS) were used to covalently bind these two biomolecules onto the surface of silicon dioxide wafers, which mimic the surface of silicon-based implantable neural probes. After covalent binding of the biomolecules, polyethylene glycol (PEG)-NH(2) was used to cap the unreacted GMBS groups.

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

Zhao X1, Pan F, Garcia-Gancedo L, Flewitt AJ, Ashley GM, Luo J, Lu JR. 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.

3.High-throughput analysis of GST-fusion protein expression and activity-dependent protein interactions on GST-fusion protein arrays with a spectral surface plasmon resonance biosensor.

Jung JW1, Jung SH, Kim HS, Yuk JS, Park JB, Kim YM, Han JA, Kim PH, Ha KS. Proteomics. 2006 Feb;6(4):1110-20.

We modified gold arrays with a glutathione (GSH) surface, and investigated high-throughput protein interactions with a spectral surface plasmon resonance (SPR) biosensor. We fabricated the GSH exterior on gold surfaces by successive modification with aminoethanethiol, 4-maleimidobutyric acid N-hydroxysuccinimide ester and GSH. We immobilized GST-Rac1, GST-RhoA, the GST-Rho-binding domain of rhotekin and the GST-p21-binding domain of PAK1 onto the GSH surface, and observed specific antigen-antibody interactions on the GST-fusion protein arrays. We determined the expression of GST-fusion proteins in Escherichia coli on the GSH surface with the SPR biosensor. We then analyzed the interactions of tissue transglutaminase (tTGase), a Ca2+-dependent enzyme, with RhoA and Rac1 on the GST-fusion protein arrays with the SPR biosensor. We found that tTGase interacted with RhoA and Rac1 in a Ca2+-dependent manner, indicating that the interactions were dependent on tTGase activity.

4.Use of reconstituted influenza virus virosomes as an immunopotentiating delivery system for a peptide-based vaccine.

Pöltl-Frank F1, Zurbriggen R, Helg A, Stuart F, Robinson J, Glück R, Pluschke G. Clin Exp Immunol. 1999 Sep;117(3):496-503.

Immunopotentiating reconstituted influenza virosomes (IRIV) were used as a delivery system for the synthetic peptide-based malaria vaccine SPf66. The reduced SPf66 peptide molecules containing terminal cysteine residues were covalently attached to phosphatidylethanolamine with the heterobifunctional crosslinker gamma-maleimidobutyric acid N-hydroxysuccinimide ester. The SPf66-phosphatidylethanolamine was incorporated into IRIV and BALB/c mice were immunized twice by intramuscular injection with peptide-loaded virosomes. Titres of elicited anti-SPf66 IgG were determined by ELISA. These titres were significantly higher and the required doses of antigen were lower, when mice had been preimmunized with a commercial whole virus influenza vaccine. After preimmunization with the influenza vaccine, SPf66-IRIV elicited far more consistently anti-SPf66 antibody responses than SPf(66)n adsorbed to alum. MoAb produced by four B cell hybridoma clones derived from a SPf66-IRIV-immunized mouse cross-reacted with Plasmodium falciparum blood stage parasites in immunofluorescence assays.