SDS of cas: 139115-91-6In 2021 ,《Conjugate of thiol and guanidyl units with oligoethylene glycol linkage for manipulation of oxidative protein folding》 was published in Molecules. The article was written by Okada, Shunsuke; Matsusaki, Motonori; Okumura, Masaki; Muraoka, Takahiro. The article contains the following contents:
Oxidative protein folding is a biol. process to obtain a native conformation of a protein through disulfide-bond formation between cysteine residues. In a cell, disulfide-catalysts such as protein disulfide isomerase promote the oxidative protein folding. Inspired by the active sites of the disulfide-catalysts, synthetic redox-active thiol compounds have been developed, which have shown significant promotion of the folding processes. In our previous study, coupling effects of a thiol group and guanidyl unit on the folding promotion were reported. Herein, we investigated the influences of a spacer between the thiol group and guanidyl unit. A conjugate between thiol and guanidyl units with a diethylene glycol spacer (GdnDEG-SH) showed lower folding promotion effect compared to the thiol-guanidyl conjugate without the spacer (GdnSH). Lower acidity and a more reductive property of the thiol group of GdnDEG-SH compared to those of GdnSH likely resulted in the reduced efficiency of the folding promotion. Thus, the spacer between the thiol and guanidyl groups is critical for the promotion of oxidative protein folding. The experimental part of the paper was very detailed, including the reaction process of tert-Butyl (2-(2-hydroxyethoxy)ethyl)carbamate(cas: 139115-91-6SDS of cas: 139115-91-6)
tert-Butyl (2-(2-hydroxyethoxy)ethyl)carbamate(cas: 139115-91-6) belongs to ethers.Oxygen is more electronegative than carbon, thus the alpha hydrogens of ethers are more acidic than those of simple hydrocarbons. They are far less acidic than alpha hydrogens of carbonyl groups (such as in ketones or aldehydes), however. SDS of cas: 139115-91-6
Referemce:
Ether – Wikipedia,
Ether | (C2H5)2O – PubChem