62558-67-2

Usage

Uses

Used in Pharmaceutical Industry:
4-(4'-hydroxy-phenylaMino)-4-oxo-butanoic acid is used as a key intermediate in the development of new drugs and therapies. Its unique structure and properties make it a promising candidate for the treatment of various medical conditions.
Used in Antioxidant Applications:
4-(4'-hydroxy-phenylaMino)-4-oxo-butanoic acid is used as an antioxidant agent for its potential role in neutralizing harmful free radicals and preventing oxidative stress-related diseases. Its antioxidant properties are currently being studied for their potential therapeutic benefits.
Used in Materials Science:
In the field of materials science, 4-(4'-hydroxy-phenylaMino)-4-oxo-butanoic acid is used as a building block for the synthesis of novel materials with unique properties. Its chemical structure allows for the development of new materials with potential applications in various industries.
Used in Biotechnology:
4-(4'-hydroxy-phenylaMino)-4-oxo-butanoic acid is used in biotechnology for its potential role in the development of new biological tools and techniques. Its unique chemical properties make it a valuable component in the creation of innovative biotechnological solutions.
Overall, 4-(4'-hydroxy-phenylaMino)-4-oxo-butanoic acid, or HOPABA, is a versatile chemical compound with a wide range of potential applications across various industries. Ongoing research and development efforts are focused on harnessing its unique properties to create new solutions and advancements in medicine, materials science, and biotechnology.

Upstream product

• 932-98-9 1-chloro-4-nitroso-benzene 
• 305-72-6 α-ketoglutaric acid disodium salt 
• 328-50-7 α-ketoglutaric acid 
• 108-30-5 succinic acid anhydride 
• 123-30-8 4-amino-phenol 

Downstream Products

• 10187-21-0 4-(pyrrolidine-2,5–dione–1-yl)phenol 
• 1303982-62-8 C₃₀H₃₁N₅O₆ 

Relevant academic research and scientific papers

An approach for differentiating isozymes. Construction of libraries containing short aromatic peptides as part of a method to design selective inhibitors against lipases

Through synthesis and assays of peptidyl substrates, we could select substrates having peptidyl complementary against lipases. The best substrate showed 20-fold improved Km relative to non-peptidyl substrate. Using this information, we generated selective inhibitors. Lipase activities with peptidyl substrates were represented as fingerprints. Differences in fingerprints reflect different structures near active site of lipases, could be used for generating selective inhibitors.

Selective α-glucosidase substrates and inhibitors containing short aromatic peptidyl moieties

We constructed a library of sugar-dipeptide conjugate to find out the best complementary against hydrophobic pocket of α-glucosidase. The best substrate showed 150-fold improved Km value relative p-acetaminophenyl-α-d-glucopyranoside for α-glucosidase from Bacillus stearothermophillus. Using information from the complementary, we synthesized sp-WY and β-Glc-sp-WY, which selectivity inhibited the cognate enzyme.

Chemoselective acylation of amines in aqueous media

Amines are efficiently acylated by both cyclic and acyclic anhydrides by dissolving them in an aqueous medium with the help of a surfactant, sodium dodecyl sulfate (SDS). Cyclic and acyclic anhydrides react with equal ease with an amine, and amines with various stereo-electronic factors react at the same rates with an anhydride. Chemoselective acylation of amines in the presence of phenols and thiols and of thiols in the presence of phenols has been achieved. No acidic or basic reagents are used during the reaction. No Chromatographic separation is required for isolation of the acylated products. Reactions in a neutral aqueous medium, easy isolation of products, and innocuous by-products make the present method a green chemical process. Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2004.

Reversible and irreversible inhibitory activity of succinic and maleic acid derivatives on acetylcholinesterase

Aryl succinic and maleic acid derivatives are potent inhibitors of bovine acetylcholinesterase in vitro. Succinic acid aminophenol derivatives 1b-e and 2b-d act as reversible inhibitors of acetylcholinesterase, while maleic acid aminophenol derivatives 3b-d and 4c-e act as choline subsite-directed irreversible inhibitors, detected by dialysis in the presence of edrophonium. Linear relationships between the logarithm of the velocity of hydrolysis of acetylcholine plotted against the time of incubation at several different inhibitor concentrations were determined. The Ki for reversible competitive inhibitors was determined. For irreversible inhibitors the Ki for the dissociation constant of the enzyme-inhibitor complex at the beginning of the recognition process was also determined as well as the inactivation constant of the enzyme-inhibitor adduct formation k+2 and the bimolecular inhibition constant ki for the inhibition of acetylcholinesterase by aminophenol derivatives 3b-d and 4c-e. The conclusions of this study can be summarized as follows for both families: (a) the aromatic moiety played a critical role in the recognition of the active site; (b) in case of the reversible inhibitor, when the ester function took the place of the hydroxyl fragment, there was an important increase in the affinity; and (c) the distance between phenolic hydroxyl and nitrogen was critical because the inhibition is ortho?metapara.

Symmetric, monofunctionalised polymethine dyes labelling reagents

A symmetric cyanine of the formula: wherein:X is selected from the group consisting of O, S and C(CH3)2;W represents non-metal atoms required to form a benzo-condensed or a naphto-condensed ring;R1 is selected from the group consisting of (CH2)nCH3, (CH2)nSO3- and (CH2)nSO3H, wherein n is an integer selected from 0 to 6 when R1 is (CH2)nCH3, and n is an integer selected from 3 to 6 when R1 is (CH2)nSO3- or (CH2)nSO3H;R2 and R3 are independently selected from the group consisting of H, a sulphonic moiety and a sulphonate moiety;Q is selected from the group consisting of:wherein q is 0 or 1 and D is selected from the group consisting of:-C≡C-G; andwherein A is O or S and G is, or contains a N, O or S nucleophile moiety or is, or contains a moiety capable of reacting with N, O or S nucleophiles.

Symmetric, monofunctionalised polymethine dyes labelling reagents

A symmetric cyanine of the formula: wherein:X is selected from the group consisting of O, S and C(CH3)2;W represents non-metal atoms required to form a benzo-condensed or a naphto-condensed ring;R1 is selected from the gro

1H and 13C NMR spectra for a series of arylmaleamic acids, arylmaleimides, arylsuccinamic acids and arylsuccinimides

The 1H and 13C NMR spectra of 17 succinic anhydride derivatives and 25 maleic anhydride derivatives were completely assigned using one- and two-dimensional NMR techniques. Copyright

Spectrophotometric and Titrimetric Determination of Carboxylic Acid Anhydrides

Two redox methods are described for the determination of carboxylic acid anhydrides involving reaction with either an excess of 4-aminophenol or a measured but excessive amount of sulfanilamide and photometric titration of N-acyl-4-aminophenol with 2-iodylbenzoate by measuring the absorbance of orange-red product at 444 nm or the residual amount of sulfanilamide is determined by titration with chloramine-T in the presence of acidified potassium bromide using methyl red as visual indicator.Mixtures of certain anhydrides have also been analyzed by the 2-iodylbenzoate method.The methods are rapid, precise, and accurate.No correlation is needed if carboxylic and mineral acids are also present.Carboxylic acid chlorides also react quantitatively.

Hydroxamic Acid Production and Active-site Induced Bamberger Rearrangement from the Action of α-Ketoglutarate Dehydrogenase on 4-Chloronitrosobensene

THe α-ketoglutarate dehydrogenase complex obtained from E. coli has been found to convert 4-chloronitrosobenzene (3) into N-(4-chlorophenyl)succinohydroxamic acid (4) and N-(4-chloro-2-hydroxyphenyl)succinamic acid (5).The conversion of 4-chloronitrosobenzene (3) into these two products is not quantitative and attempts to identify other, significant low-molecular-weight metabolites have been unsuccessful.Partial enzyme-inactivation has been observed during the incubation of 4-chloronitrosobensene (3) with α-ketoglutarate dehydrogenase.The direct enzymic conversion of the hydroxamic acid (4) into the isomeric product (5) did not occur.These results are interpreted on the basis of a mechanism in which N-(4-chlorophenyl)hydroxylamine (6) is generated at the enzyme active-site by a redox process.Condensation of the active-site bound products would give rise to the hydroxamic acid (4) directly, while a Bamberger-like rearrangement of the active-site bound hydroxylamine(6), followed by condensation of the resulting o-aminophenol, would explain the production of the succinamic acid.