Synthesis and Biological Activity of Unsymmetrical Monoterpenylhetaryl Disulfides
New unsymmetrical monoterpenylhetaryl disulfides based on heterocyclic disulfides and monoterpene thiols were synthesized for the first time in 48–88% yields.
D V Sudarikov +2 more
exaly +3 more sources
A novel method for the mechanochemical synthesis of unsymmetrical disulfides using phosphorodithioic acid derivatives [PDF]
In this study, we report the efficient synthesis of unsymmetrical disulfides using a mechanochemical ball-milling approach. This research successfully yielded alkyl-alkyl, alkyl-aryl, and aryl-aryl unsymmetrical disulfides without any detectable ...
Mikołaj Walter +4 more
doaj +2 more sources
Photocatalytic Bilateral Disulfuration of Thioethers Toward α‐Sulfide Disulfides With Antibacterial Activity [PDF]
α−Sulfide disulfides represent valuable motifs in organic and pharmaceutical chemistry. However, the limited availability of synthetic approaches for α−sulfide disulfides has impeded progress in this field.
Qingqiang Tian +4 more
doaj +2 more sources
Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols [PDF]
Thiol isomerases are a family of enzymes that participate in oxidative protein folding. They contain highly reactive vicinal thiols in a CXXC motif within their catalytic domains to mediate thiol-disulfide switching as part of their reductase, oxidase ...
Osamede C. Owegie +3 more
doaj +2 more sources
Synthesis of disulfides and 3-sulfenylchromones from sodium sulfinates catalyzed by TBAI [PDF]
A new synthetic method for disulfides and 3-sulfenylchromones is reported. This innovative approach is based on the tetrabutylammonium iodide (TBAI)/H2SO4 reduction system using sodium sulfinate as key component, thus eliminating the need for thiols and ...
Zhenlei Zhang +6 more
doaj +2 more sources
Identification of allosteric disulfides from labile bonds in X-ray structures [PDF]
Protein disulfide bonds link pairs of cysteine sulfur atoms and are either structural or functional motifs. The allosteric disulfides control the function of the protein in which they reside when cleaved or formed.
Aster E. Pijning +4 more
doaj +1 more source
NO, thiols and disulfides [PDF]
The chemical nature of the messenger molecule, nitric oxide (NO), and especially its reactivity towards thiol groups and disuifides, could explain, at least partly, its intervention in so many different biological processes. NO can be regarded as the smallest molecule suitable for electron transport in biological systems. The S‐nitrosation reaction and
Girard, Pierre, Potier, Pierre
openaire +2 more sources
Lattice Imaging of Self-Assembled Monolayers of Partially Fluorinated Disulfides and Thiols on Sputtered Gold by Atomic Force Microscopy [PDF]
The structure of self-assembled monolayers (SAMs) of various fluorinated disulfides, perfluoroalkylamide thiols, and a mixed alkyl perfluoroalkylamide disulfide on sputtered gold was studied by atomic force microscopy (AFM).
Schönherr, H., Vancso, G.J.
core +10 more sources
Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles [PDF]
Disulfide bonds are required for the stability and function of a large number of proteins. Recently, the results from genome analysis have suggested an important role for disulfide bonds concerning the structural stabilization of intracellular proteins from hyperthermophilic Archaea and Bacteria, contrary to the conventional view that structural ...
Rudolf, Ladenstein, Bin, Ren
openaire +2 more sources
The effect of tensile stress on the conformational free energy landscape of disulfide bonds. [PDF]
Disulfide bridges are no longer considered to merely stabilize protein structure, but are increasingly recognized to play a functional role in many regulatory biomolecular processes.
Padmesh Anjukandi +3 more
doaj +1 more source

