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

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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
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.
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