5776-78-3

Basic information

• Product Name: HEXANOICACID,6-[[6-[(6-AMINO-1-OXOHEXYL)AMINO]-1-OXOHEXYL]AMINO]-
• Synonyms: HEXANOICACID,6-[[6-[(6-AMINO-1-OXOHEXYL)AMINO]-1-OXOHEXYL]AMINO]-;6-(6-(6-aminohexanamido)hexanamido)hexanoic acid
• CAS NO: 5776-78-3
• Molecular Formula: C18H35N3O4
• Molecular Weight: 357.4882
• Mol File: 5776-78-3.mol
• Article Data: 1

Chemical Properties

• Melting Point: 218-220 °C
• Boiling Point: 659.8±50.0 °C(Predicted)
• Appearance: /
• Density: 1.064±0.06 g/cm3(Predicted)
• Storage Temp.: Refrigerator
• Solubility: Aqueous Acid (Slightly), Methanol (Slightly), Water (Slightly)
• PKA: 4.75±0.10(Predicted)
• CAS DataBase Reference: HEXANOICACID,6-[[6-[(6-AMINO-1-OXOHEXYL)AMINO]-1-OXOHEXYL]AMINO]-(CAS DataBase Reference)
• NIST Chemistry Reference: HEXANOICACID,6-[[6-[(6-AMINO-1-OXOHEXYL)AMINO]-1-OXOHEXYL]AMINO]-(5776-78-3)
• EPA Substance Registry System: HEXANOICACID,6-[[6-[(6-AMINO-1-OXOHEXYL)AMINO]-1-OXOHEXYL]AMINO]-(5776-78-3)

Safety Data

• Hazardous Substances Data: 5776-78-3(Hazardous Substances Data)

Usage

Description

HEXANOICACID,6-[[6-[(6-AMINO-1-OXOHEXYL)AMINO]-1-OXOHEXYL]AMINO]is a complex organic compound with a unique structure that features a hexanoic acid backbone and multiple amino and oxo groups. HEXANOICACID,6-[[6-[(6-AMINO-1-OXOHEXYL)AMINO]-1-OXOHEXYL]AMINO]is characterized by its ability to form preconjugates, which are essential in various immunoassay techniques and the synthesis of coupling agents.

Uses

Used in Diagnostics Industry:
HEXANOICACID,6-[[6-[(6-AMINO-1-OXOHEXYL)AMINO]-1-OXOHEXYL]AMINO]is used as a preconjugate in the development of immunoreactive conjugates. These conjugates are useful as developer antigens in competitive inhibition immunoassays for the detection and quantification of polymorphic analytes. This application is particularly relevant in the field of diagnostics, where accurate and sensitive detection of specific biomarkers is crucial for disease diagnosis and monitoring.
Used in Pharmaceutical Industry:
HEXANOICACID,6-[[6-[(6-AMINO-1-OXOHEXYL)AMINO]-1-OXOHEXYL]AMINO]is also used in the efficient synthesis of heterobifunctional coupling agents. These agents are essential in the development of novel drug delivery systems and the creation of new pharmaceutical compounds. By facilitating the formation of covalent bonds between different molecules, this compound plays a vital role in the advancement of drug design and development, ultimately contributing to the discovery of new therapeutic agents and treatments for various medical conditions.

Upstream product

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Relevant articles and documents

Enzymatic synthesis of nylon-6 units in organic solvents containing low concentrations of water

NylB′ carboxylesterase, which is 88% homologous to functional 6-aminohexanoate-dimer hydrolase (NylB) from Arthrobacter sp., possesses trace synthetic activity [0.0004μmolmin-1mg-1 (U/mg)] from 6-aminohexanoate (Ahx) to its oligomers in 90% tert-butyl alcohol. The synthetic activity and the ratio of the synthetic activity to the hydrolytic activity were significantly affected by amino acid substitutions at positions 181, 266 and 370. The synthetic activity was enhanced to 2.7U/mg by G181D-H266N substitutions, and the activity was further enhanced in the G181D-H266N-D370Y triple mutant to a level approximately 104-fold greater than the parental carboxylesterase form (3.4U/mg), which was nearly equal to the ordinary hydrolytic activity in water (type A-mutants). Type A-mutants possessed more than 50% of the 6-aminohexanoate-linear dimer (Ald)-hydrolytic activity at 0-70% tert-butyl alcohol, but the synthetic reaction became predominant at 85-90% tert-butyl alcohol. In contrast, type B-mutants (G181E-H266N and G181N-H266N) possessed quite low levels of Ald-hydrolytic activity (a type C-mutant (R187S-F264C-D370Y), the Ald-hydrolytic activity was enhanced to approximately 80-fold that of the parental carboxylesterase, but the mutant barely demonstrated any synthetic activity. On the basis of the three-dimensional structure of the Ald-bound enzyme and a kinetic study for typical mutant enzymes, we propose that the efficient enzymatic syntheses of nylon-6 units were achieved by (i) stable binding of the 1st-Ahx at the N-terminal region with Asp181, (ii) interaction of the 2nd-Ahx at the C-terminal region with Tyr370, and (iii) motion of Tyr170 that generated a closed form in the catalytic center of Ald hydrolase.