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Application Area

Fmoc-S-acetamidomethyl-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

Fmoc-Amino Acids

Catalog number

BAT-000427

CAS number

182410-75-9

Molecular Formula

C25H25N3O7S

Molecular Weight

511.54

IUPAC Name

(2,5-dioxopyrrolidin-1-yl) (2R)-3-(acetamidomethylsulfanyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)propanoate

Synonyms

Fmoc-L-Cys(Acm)-OSu

Appearance

Off-white powder

Purity

≥ 98% (HPLC)

Melting Point

145-153 °C

Storage

Store at 2-8 °C

InChI

InChI=1S/C25H25N3O7S/c1-15(29)26-14-36-13-21(24(32)35-28-22(30)10-11-23(28)31)27-25(33)34-12-20-18-8-4-2-6-16(18)17-7-3-5-9-19(17)20/h2-9,20-21H,10-14H2,1H3,(H,26,29)(H,27,33)/t21-/m0/s1

InChI Key

LKULFXHPZSDOLA-NRFANRHFSA-N

Canonical SMILES

CC(=O)NCSCC(C(=O)ON1C(=O)CCC1=O)NC(=O)OCC2C3=CC=CC=C3C4=CC=CC=C24

Fmoc-S-acetamidomethyl-L-cysteine N-hydroxysuccinimide ester, commonly known as Fmoc-Cys(Acm)-OSu, is a versatile chemical reagent utilized primarily in protein and peptide research. Explore the diverse applications of Fmoc-Cys(Acm)-OSu:

Protein Synthesis: Delving into solid-phase peptide synthesis (SPPS), researchers leverage Fmoc-Cys(Acm)-OSu for seamlessly integrating cysteine residues into peptides. The Fmoc protection group facilitates meticulous stepwise peptide assembly while safeguarding against unwanted side reactions. With the S-acetamidomethyl (Acm) shield maintaining the integrity of cysteine thiol groups until specific deprotection steps, precision in protein synthesis is paramount.

Peptide Labeling: Unveiling the capabilities of the NHS ester within Fmoc-Cys(Acm)-OSu, researchers unlock efficient and selective peptide labeling with reporter molecules or fluorescent tags. This application is a cornerstone for investigating peptide interactions, localization, and dynamics within biological systems. Fluorescently labeled peptides become invaluable tools for imaging techniques and binding assays, enhancing our understanding of molecular interactions.

Site-Specific Conjugation: Harnessing the power of Fmoc-Cys(Acm)-OSu, scientists strategically introduce cysteine residues at designated sites in peptides and proteins for targeted conjugation purposes. This strategic maneuver enables the attachment of diverse functional groups or molecules like drugs, polymers, or other proteins. By achieving site-specific conjugation, researchers maintain precise control over the modification process, opening new avenues for tailored molecular interactions.

Protein Cross-Linking: Embracing the potential of Fmoc-Cys(Acm)-OSu in cross-linking studies, researchers unravel the intricacies of protein-protein or protein-ligand interactions. The incorporated cysteine residues act as reactive sites for forging disulfide bonds or other covalent linkages, illuminating the structural landscape of proteins. This technique plays a vital role in structural biology, mapping interaction domains and fortifying protein complexes, furthering our comprehension of molecular interactions.

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. 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.

3. Fmoc N-hydroxysuccinimide ester: A facile and multifunctional role in N-glycan analysis

Chang Wang, Yike Wu, Sheng Liu, Liang Zhang, Bi-Feng Liu, Xin Liu Anal Chim Acta. 2020 Sep 22;1131:56-67. doi: 10.1016/j.aca.2020.07.044. Epub 2020 Jul 30.

N-glycans that are fluorescently tagged by glycosylamine acylation have become a promising way for glycan biomarker discovery. Here, we describe a simple and rapid method using Fmoc N-hydroxysuccinimide ester (Fmoc-OSu) to label N-glycans by reacting with their corresponding intermediate glycosylamines produced by microwave-assisted deglycosylation. After optimizing reaction conditions, this derivatization reaction can be effectively achieved under 40 °C for 1 h. Moreover, the comparison of fluorescent intensities for Fmoc-OSu, Fmoc-Cl and 2-AA labeling strategies were also performed. Among which, the fluorescent intensities of Fmoc-OSu labeled glycan derivatives were approximately 5 and 13 times higher than that labeled by Fmoc-Cl and 2-AA respectively. Furthermore, the developed derivatization strategy has also been applied for analyzing serum N-glycans, aiming to screen specific biomarkers for early diagnosis of lung squamous cell cancer. More interestingly, the preparation of free reducing N-glycan standards have been achieved by the combination of HPLC fraction of Fmoc labeled glycan derivatives and Fmoc releasing chemistry. Overall, this proposed method has the potential to be used in functional glycomic study.