5325-76-8

Basic information

• Product Name: 4,4'-DITHIOBISPHENYLACETIC ACID
• Synonyms: 4,4'-DITHIOBISPHENYLACETIC ACID;4,4'-DITHIOBISBENZENEACETIC ACID, DISULFIDE;(Dithiodi-p-phenylene)di-acetic Acid;NSC 211;NSC 38071
• CAS NO: 5325-76-8
• Molecular Formula: C₁₆H₁₄O₄S₂
• Molecular Weight: 334.41
• Product Categories: Sulfur & Selenium Compounds
• Mol File: 5325-76-8.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 549.4°Cat760mmHg
• Flash Point: 286.1°C
• Appearance: /
• Density: 1.44g/cm³
• Storage Temp.: -20°C Freezer
• Solubility: Acetonitrile (Slightly), DMSO (Slightly), Methanol (Slightly)
• CAS DataBase Reference: 4,4'-DITHIOBISPHENYLACETIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: 4,4'-DITHIOBISPHENYLACETIC ACID(5325-76-8)
• EPA Substance Registry System: 4,4'-DITHIOBISPHENYLACETIC ACID(5325-76-8)

Safety Data

• Hazardous Substances Data: 5325-76-8(Hazardous Substances Data)

Usage

Uses

A redox buffer that increases the folding rate of disulfide-containing proteins realative to traditional buffers such as glutathione and glutathione-disulfide.

Upstream product

• 824-46-4 methoxyhydroquinone 
• 39161-84-7 4-mercaptophenylacetic acid 
• 95-71-6 2-methylbenzene-1,4-diol 

Relevant articles and documents

Folding disulfide-containing proteins faster with an aromatic thiol

The traditional method for in vitro folding of disulfide-containing proteins is slow and involves a redox buffer of glutathione and glutathione disulfide. To increase the folding rate and to gain insight into the folding process, we replaced glutathione, an aliphatic thiol, with a commercially available aromatic thiol, 4-mercaptobenzeneacetate (1). Aromatic thiol 1 was selected due to its enhanced nucleophilicity and its enhanced leaving-group ability relative to glutathione at pH 7.7. To demonstrate the advantages of 1, the folding of reduced and scrambled RNase A at pH 7.0 and 7.7 in the presence of 1 and glutathione was investigated. For each set of folding conditions, the optimum concentration of each thiol was initially determined and then the folding rates in the presence of each thiol were measured concurrently. In all cases examined, the folding rate enhancement with the aromatic thiol was 5- 6-fold. Furthermore, under similar conditions folding rates were almost identical with either reduced or scrambled RNase A. In addition the 5-6-fold folding rate enhancement varied only slightly with pH, 7.0 vs 7.7.

METHOD FOR PATHOGENS, MICROORGANISMS, AND PARASITES INACTIVATION

The invention provides a method for inactivation or reduction of pathogens, microorganisms or parasites in a sample, media, composition, utility, device, surface or organism by treatment with an alkylating compound of Structure I, followed by elimination or reduction of the residual compound with Structure I by treatment with a neutralizing agent, which eliminates or reduces the toxicity or other undesirable properties of the alkylating compound with Structure I. The neutralizing agent may be present in a treatment solution or be part of a solid-phase agent, and preferably acts by eliminating the alkylating properties of the compound of Structure I.

Enzymatic thiol Michael addition using laccases: Multiple C-S bond formation between p-hydroquinones and aromatic thiols

Laccases create C-C, C-O or C-N bonds and have been investigated intensively as catalysts for green chemistry and white biotechnology. However, little is known about C-S bond formation in laccase-catalyzed reactions. We have used the laccases from Pycnopo