Carbon Disulfide Adduct

Carbon disulfide adducts are molecular species formed when carbon disulfide (CS₂) combines with another molecule, ion, or metal center through new interactions or chemical bonds. In common reactions, an electron-rich nucleophile attacks the electrophilic carbon atom of CS₂, while the sulfur atoms stabilize the resulting charge and participate in coordination or further reaction. These adducts can include dithiocarbonate, dithiocarbamate, and metal-associated structures, depending on the reacting partner and conditions. Studying their formation, bonding, and reactivity supports organic synthesis, inorganic and coordination chemistry, reaction mechanism analysis, and the design of sulfur-containing materials.

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Research

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Source: Chen, Z., et al. Making Conjugation-induced Fluorescent PEGylated Virus-like Particles by Dibromomaleimide-disulfide Chemistry. J. Vis. Exp. (2018)This video demonstrates the fluorescent functionalization of virus-like particles by re-bridging reduced disulfides with a polyethylene glycol (PEG) linker, producing stable, trackable conjugates suitable for cellular imaging and targeted delivery in biomedical applications.

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Lasers are frequently used in studies of the cellular response to DNA damage. However, they generate lesions whose spacing, frequency, and collisions with replication forks are rarely characterized. Here, we describe an approach that enables the determination of these parameters with laser localized interstrand crosslinks.

Making Conjugation-induced Fluorescent PEGylated Virus-like Particles by Dibromomaleimide-disulfide Chemistry

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Cited by 12 •

2018

Here, we present a procedure to fluorescently functionalize the disulfides on Qβ VLP with dibromomaleimide. We describe Qβ expression and purification, the synthesis of dibromomaleimide-functionalized molecules, and the conjugation reaction between dibromomaleimide and Qβ. The resulting yellow fluorescent conjugated particle can be used as a fluorescence probe inside cells.

Non-Reducing SDS PAGE: A Method to Analyze Disulfide-Linked Multimeric Protein Complexes

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2025

This video describes the technique of separating the protein samples by non-reducing SDS-PAGE to analyze the multimeric protein complexes. This technique retains the multimer subunits of a protein held by the disulfide bonds which can later be analyzed by western blotting.

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