Disulfide Crosslinking
Disulfide Crosslinking - Related Videos
03:51
Fluorescent Functionalization of Virus-Like Particles via Disulfide Re-bridging
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2026
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.
03:47
Crosslinking Neuronal Surface Proteins in the Mouse Brain using a Chemical Crosslinking Assay
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2025
This video demonstrates the crosslinking of neuronal surface proteins using Bis-sulfosuccinimidyl suberate or BS3. Isolated and chilled mouse brain is sectioned coronally. The desired region is extracted from the sections, minced, and treated with BS3. BS3 crosslinks surface proteins like GABA receptors, leaving internal proteins unaltered. The reaction is quenched with glycine before processing the samples for further analysis.
11:15
Nanosponge Tunability in Size and Crosslinking Density
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Cited by 1 •
2017
This article describes a process for tuning the size and crosslinking density of covalently crosslinked nanoparticles from linear polyesters containing pendant functionality. By tailoring synthesis parameters (polymer molecular weight, pendant functionality incorporation, and crosslinker equivalents), a desired nanoparticle size and crosslinking density can be achieved for drug delivery applications.
09:37
Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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Cited by 2 •
2019
Disulfide linkages have long been known to stabilize the structure of many proteins. A simple method to analyze multimeric complexes stabilized by these linkages is through non-reducing SDS-PAGE analysis. Here, this method is illustrated by analyzing the nuclear isoform of dUTPase from the human bone osteosarcoma cell line U-2 OS.
10:18
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.
FAQs
The key chemical event is oxidation of two thiol groups into a sulfur-sulfur linkage. In this redox step, hydrogen or reducing equivalents are released, so the local sulfur chemistry changes from separate functional groups to a covalent connection between chains. That transformation links molecular architecture to increased structural stability and provides a specific redox-controlled chemical change to study.
Reducing conditions reverse the network-forming step by cleaving disulfide bonds. This reversibility allows a material's structure to respond to its chemical environment rather than remaining permanently fixed. Switching between oxidizing and reducing conditions can therefore tune whether chains remain connected, producing corresponding changes in strength, solubility, and mechanical behavior.
Thiol availability is a central molecular variable because each disulfide connection requires two thiol groups. The extent to which chains become connected therefore depends on whether suitable sulfur-containing groups can participate in oxidation. In chemistry studies, this relationship helps explain why related systems may form different network structures and why their resulting properties can vary.
Network formation changes more than molecular connectivity: it can alter how a system behaves as a material. Covalent links can increase structural stability while also changing solubility and mechanical properties. Because reducing conditions can remove those links, researchers can investigate how much of each property comes from the crosslinked architecture rather than from the unlinked molecular chains.
A basic study begins with a system containing thiol groups, allows oxidation to generate disulfide connections, and then evaluates the resulting structure or properties. A reducing treatment can serve as a reversal step, testing whether the observed changes depend on the disulfide network. Comparing oxidized and reduced states reveals the contribution of reversible crosslinking.
This approach is useful when a material must combine structural reinforcement with chemical adjustability. Oxidation can stabilize the system through disulfide formation, whereas reduction can cleave the connections. That controllable behavior makes the chemistry relevant to stimuli-responsive materials, biomaterials, and polymer systems whose strength, solubility, or mechanical properties need to respond to conditions.
Changes in strength, solubility, or mechanical properties indicate how covalent connections influence the larger network. If those changes diminish after reduction, the comparison supports a link between the measured behavior and disulfide connectivity. Such results connect molecular sulfur chemistry with observable material performance and help assess the structural consequences of reversible crosslinking.
Sulfur-containing functional groups can connect portions of protein-based structures through disulfide bonds, helping regulate their architecture and stability. Because these bonds respond to redox conditions, chemical studies can examine how changing the surrounding conditions affects organization and behavior. This provides a bridge between molecular bonding, protein-based materials, and biomaterial design.