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Application Area

Boc-S-4-methylbenzyl-L-cysteine N-hydroxysuccinimide ester

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

BOC-Amino Acids

Catalog number

BAT-002886

CAS number

140842-91-7

Molecular Formula

C20H26N2O6S

Molecular Weight

422.50

Boc-S-4-methylbenzyl-L-cysteine N-hydroxysuccinimide ester

IUPAC Name

(2,5-dioxopyrrolidin-1-yl) (2R)-3-[(4-methylphenyl)methylsulfanyl]-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoate

Synonyms

Boc-L-Cys(pMeBzl)-Osu; (R)-2,5-Dioxopyrrolidin-1-yl 2-((tert-butoxycarbonyl)amino)-3-((4-methylbenzyl)thio)propanoate

Appearance

White powder

Purity

≥ 98% (HPLC)

Melting Point

90-97 °C

Storage

Store at 2-8°C

InChI

InChI=1S/C20H26N2O6S/c1-13-5-7-14(8-6-13)11-29-12-15(21-19(26)27-20(2,3)4)18(25)28-22-16(23)9-10-17(22)24/h5-8,15H,9-12H2,1-4H3,(H,21,26)/t15-/m0/s1

InChI Key

JMTFQOBMHSNDOP-HNNXBMFYSA-N

Canonical SMILES

CC1=CC=C(C=C1)CSCC(C(=O)ON2C(=O)CCC2=O)NC(=O)OC(C)(C)C

Boc-S-4-methylbenzyl-L-cysteine N-hydroxysuccinimide ester plays a crucial role in organic synthesis, specifically in peptide chemistry. Here are four key applications of this compound:

Peptide Synthesis: At the forefront of solid-phase peptide synthesis, Boc-S-4-methylbenzyl-L-cysteine N-hydroxysuccinimide ester is a game-changer. By enabling the incorporation of cysteine residues into peptides, it facilitates the formation of stable peptide bonds essential for crafting peptides with precise sequences and functional properties. This process is instrumental in the creation of peptides with diverse applications in various fields.

Protein Engineering: Delving into the realm of protein modification, this compound plays a pivotal role in shaping modified peptides and proteins. Through strategic deprotection and coupling reactions, researchers can introduce modified cysteine residues, paving the way for site-specific conjugation of functional groups. This approach propels the development of proteins with tailored functionalities, catering to the intricate needs of both research and therapeutic endeavors.

Drug Development: In the dynamic landscape of pharmaceuticals, Boc-S-4-methylbenzyl-L-cysteine N-hydroxysuccinimide ester stands as a linchpin in the synthesis of peptide-based drug candidates. It drives the creation of peptide analogs endowed with enhanced stability and activity, essential for the development of novel therapeutic agents with superior pharmacokinetics and targeted efficacy. This compound serves as a cornerstone in the quest for innovative drug solutions.

Biosensor Development: Spearheading the arena of biosensors, this compound fuels the design and fabrication of cutting-edge sensor technologies. By integrating modified cysteine residues into sensor proteins or peptides, researchers achieve precise immobilization onto sensor surfaces, enhancing the sensitivity and specificity of biosensors crucial for diagnostics and environmental monitoring applications. This innovative approach revolutionizes the development of biosensors, opening new avenues for advanced sensing technologies.

1. Amine coupling through EDC/NHS: a practical approach

Marcel J E Fischer Methods Mol Biol. 2010;627:55-73. doi: 10.1007/978-1-60761-670-2_3.

Surface plasmon resonance (SPR) is one of the leading tools in biomedical research. The challenge in its use is the controlled positioning of one of the components of an interaction on a carefully designed surface. Many attempts in interaction analysis fail due to the non-functional or unsuccessful immobilization of a reactant onto the complex matrix of that surface. The most common technique for linking ligands covalently to a hydrophilic solid surface is amine coupling via reactive esters. In this chapter detailed methods and problem discussions will be given to assist in fast decision analysis to optimize immobilization and regeneration. Topics in focus are different coupling techniques for small and large molecules, streptavidin-biotin sandwich immobilization, and optimizing regeneration conditions.

2. General protein-protein cross-linking

Alice Alegria-Schaffer Methods Enzymol. 2014;539:81-7. doi: 10.1016/B978-0-12-420120-0.00006-2.

This protocol describes a general protein-to-protein cross-linking procedure using the water-soluble amine-reactive homobifunctional BS(3) (bis[sulfosuccinimidyl] suberate); however, the protocol can be easily adapted using other cross-linkers of similar properties. BS(3) is composed of two sulfo-NHS ester groups and an 11.4 Å linker. Sulfo-NHS ester groups react with primary amines in slightly alkaline conditions (pH 7.2-8.5) and yield stable amide bonds. The reaction releases N-hydroxysuccinimide (see an application of NHS esters on Labeling a protein with fluorophores using NHS ester derivitization).

3. Selective protein N-terminal labeling with N-hydroxysuccinimide esters

Hanjie Jiang, Gabriel D D'Agostino, Philip A Cole, Daniel R Dempsey Methods Enzymol. 2020;639:333-353. doi: 10.1016/bs.mie.2020.04.018. Epub 2020 Apr 28.

In order to gain detailed insight into the biochemical behavior of proteins, researchers have developed chemical tools to incorporate new functionality into proteins beyond the canonical 20 amino acids. Important considerations regarding effective chemical modification of proteins include chemoselectivity, near stoichiometric labeling, and reaction conditions that maintain protein stability. Taking these factors into account, we discuss an N-terminal labeling strategy that employs a simple two-step "one-pot" method using N-hydroxysuccinimide (NHS) esters. The first step converts a R-NHS ester into a more chemoselective R-thioester. The second step reacts the in situ generated R-thioester with a protein that harbors an N-terminal cysteine to generate a new amide bond. This labeling reaction is selective for the N-terminus with high stoichiometry. Herein, we provide a detailed description of this method and further highlight its utility with a large protein (>100kDa) and labeling with a commonly used cyanine dye.