1001-13-4

Usage

Uses

Used in Pharmaceutical Industry:
Butyric acid, 2-amino-4-sulfo-, is used as a pharmaceutical compound for its potential therapeutic effects. The unique structure of this molecule allows it to interact with various biological targets, making it a promising candidate for the development of new drugs. Its specific application reason in the pharmaceutical industry is due to its ability to modulate cellular processes and potentially influence disease progression.
Used in Chemical Research:
In the field of chemical research, Butyric acid, 2-amino-4-sulfo-, serves as an important building block for the synthesis of various complex molecules and compounds. Its unique structure with both amino and sulfo groups makes it a valuable tool for researchers to explore new chemical reactions and develop novel compounds with potential applications in different industries.
Used in Environmental Applications:
Butyric acid, 2-amino-4-sulfo-, can be utilized in environmental applications, such as water treatment and soil remediation, due to its ability to chelate and sequester heavy metals. The sulfo group in the molecule enhances its affinity for metal ions, making it an effective agent for removing contaminants from the environment.

InChI:InChI=1/C4H9NO5S/c5-3(4(6)7)1-2-11(8,9)10/h3H,1-2,5H2,(H,6,7)(H,8,9,10)

Upstream product

• 626-72-2 L-homocystine 
• 63-68-3 L-methionine 
• 3226-65-1 L-methionine sulfoxide 
• 6027-15-2 D-homocystine 
• 64-18-6 formic acid 
• 462-10-2 DL-homocystine 
• 7732-18-5 water 
• 7726-95-6 bromine 
• 7722-84-1 dihydrogen peroxide 

Downstream Products

• 1623054-96-5 C₃₅H₄₅N₄O₆S⁽¹⁺⁾ 

Relevant academic research and scientific papers

Under-flame Reaction of Sulfur-containing Amino Acids by a Hydrogen-Oxygen Flame

Methionine was subjected to a flame-induced reaction in water or in an aqueous formic acid solution by using a hydrogen (50%)-oxygen (50%), hydrogen (87%)-oxygen (13%) and hydrogen diffusion flame. Besides the already-known stepwise oxidation by a hydroxyl radical, the contribution of a hydrogen atom from the flame to the reaction was recognized when the hydrogen-rich mixtures were employed. Homoserine was obtained under all the reaction conditions employed here, and glutamic acid when employing aqueous formic acid as a solvent. A common intermediate, the 3-carboxy-3-aminopropyl radical, appeared to exist in the reaction pathway. A coupling reaction of this radical with a hydrogen atom, hydroxyl radical and hydroxycarbonyl radical afforded 2-aminobutyric acid, homoserine and glutamic acid, respectively. Lanthionine and S-methylcysteine underwent the same reactions. Increasing the hydrogen content of the fuel and adding formic acid to the solvent resulted in retarding the reaction rate. The latter modification of the reaction system also brought about greater stability of the reaction products.

Flame-induced reactions of sulfur-containing amino acids in an aqueous solution

Hydrogen-oxygen flames, when blown against an aqueous solution of methionine, induced conversion reactions to homoserine, 2-aminobutyric acid and glutamic acid. Besides the already-known reactions by a hydroxyl radical, a contribution of a hydrogen atom from hydrogen-rich flames to the reaction was recognized. We successfully controlled the vigorous oxidation of the system using a radical scavenger.

GLUCAGON ANALOGS EXHIBITING ENHANCED SOLUBILITY IN PHYSIOLOGICAL pH BUFFERS

Modified glucagon peptides are disclosed having improved solubility while retaining glucagon agonist activity. The glycogen peptides have been modified by substitution of native amino acids with, and/or addition of, charged amino acids to the carboxy terminus of the peptide. The modified glucagon agonists can be further modified by pegylation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 23, or both to further enhance the solubility of the glucagon agonist analogs.

GLUCAGON/GLP-1 RECEPTOR CO-AGONISTS

Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (K-RNRNNIA) and SEQ ID NO: 28 (KRNR).