Thiol Chemistry
Thiol Chemistry - Related Videos
11:17
Synthesis of Programmable Main-chain Liquid-crystalline Elastomers Using a Two-stage Thiol-acrylate Reaction
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Cited by 107 •
2016
A novel methodology is presented to synthesize and program main-chain liquid-crystalline elastomers using commercially available starting monomers. A wide range of thermomechanical properties was tailored by adjusting the amount of crosslinker, while the actuation performance was dependent on the amount of applied strain during programming.
02:33
Preparation and Reactions of Thiols
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2023
Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol. This reaction fails because the thiol product can undergo a second nucleophilic substitution reaction in the presence of an excess alkyl halide to generate a sulfide as a by-product. This limitation can be overcome by using thiourea as the nucleophile. The reaction first produces an alkyl...
08:42
Coordination Chemistry Complexes
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2023
Source: Laboratory of Dr. Neal Abrams — SUNY College of Environmental Science and Forestry Transition metals are found everywhere from vitamin supplements to electroplating baths. Transition metals also make up the pigments in many paints and compose all minerals. Typically, transition metals are found in the cationic form since they readily oxidize, or lose electrons, and are surrounded by electron donors called ligands. These ligands do not form ionic or covalent bonds with the metal center,...
02:17
Structure and Nomenclature of Thiols and Sulfides
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2023
Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry, similar...
12:31
Chemoselective Modification of Viral Surfaces via Bioorthogonal Click Chemistry
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Cited by 14 •
2012
Adenovirus particles are engineered to contain either the unnatural amino acid analogue azidohomoalanine or the azido sugar O-GlcNAz. The azide group of each is chemoselectively ligated via "click" chemistry reactions as a means of viral surface modification.
FAQs
At the sulfur atom, a cysteine thiol can act as a nucleophile and participate directly in molecular reactions. Because these residues occur within proteins, changes at a reactive cysteine can alter protein activity or interactions. This provides a mechanistic link between local chemical reactivity and broader regulation of cellular signaling and protein function.
Cellular redox conditions determine whether susceptible thiols remain reduced or undergo oxidation. Oxidation can produce disulfide bonds, while reduction can reverse that change. This reversibility allows protein states to adjust as conditions shift, making thiol-disulfide balance important during immune activation and oxidative stress, when changes in redox conditions can influence cellular responses.
Disulfide formation is especially consequential when protein architecture or molecular contacts depend on cysteine residues. In antibodies, thiol-disulfide chemistry is therefore relevant to their characteristic structure and to studying how redox changes may affect antibody-related interactions. Examining these bonds connects a specific sulfur reaction with the organization and function of immune proteins.
Researchers can measure the relative states of thiol and disulfide groups and compare them under different cellular or experimental conditions. They can also manipulate these states to test whether a change affects protein activity or interactions. This paired strategy helps distinguish an association from a functional consequence in studies of redox balance and immune signaling.
In immunology, thiol measurements can be used alongside studies of immune activation and antioxidant defenses. Comparisons across conditions can show whether altered redox balance accompanies changes in signaling proteins or protective cellular responses. Because the chemistry can affect structure, activity, and interactions, these measurements connect oxidative conditions with molecular changes in immune-system behavior.
During infection research, thiol chemistry provides a framework for examining both host and microbial proteins. Investigators can study how redox changes relate to host responses, microbial enzyme function, and interactions between pathogen and host. Manipulating thiol-disulfide states may also help evaluate therapeutic strategies, while measurements reveal molecular changes associated with oxidative stress.