21959-36-4 Usage
Description
N-Acetyl-3,5-diiodo-L-tyrosine ethyl ester, also known as (S)-Ethyl 2-acetamido-3-(4-hydroxy-3,5-diiodophenyl)propanoate, is a synthetic chemical compound with a unique molecular structure. It is derived from the modification of the naturally occurring amino acid L-tyrosine by acetylating the amino group and introducing iodine atoms at the 3 and 5 positions on the phenyl ring. The ethyl ester group further distinguishes it from its parent compound. This research chemical compound has potential applications in various fields due to its distinct properties.
Uses
Used in Pharmaceutical Research:
N-Acetyl-3,5-diiodo-L-tyrosine ethyl ester is used as a research chemical compound for pharmaceutical applications. It serves as a valuable tool in the development of new drugs and therapies, particularly in the area of hormone regulation and thyroid function. Its unique structure allows researchers to study its interactions with biological systems and explore its potential as a therapeutic agent.
Used in Thyroid Function Studies:
In the field of endocrinology, N-Acetyl-3,5-diiodo-L-tyrosine ethyl ester is used as a research chemical compound to investigate thyroid function and the role of iodine in hormone production. The presence of iodine atoms in the molecule makes it an interesting candidate for studying the uptake and utilization of iodine by the thyroid gland, which is essential for the synthesis of thyroid hormones.
Used in Radiotracer Development:
N-Acetyl-3,5-diiodo-L-tyrosine ethyl ester can be used as a precursor in the development of radiotracers for medical imaging. The incorporation of iodine atoms in the molecule makes it suitable for radiolabeling with isotopes such as iodine-123 or iodine-131. These radiotracers can be used in diagnostic procedures to visualize the thyroid gland and other tissues, aiding in the detection and monitoring of various diseases.
Used in Organic Synthesis:
In the field of organic chemistry, N-Acetyl-3,5-diiodo-L-tyrosine ethyl ester is used as a building block or intermediate in the synthesis of more complex molecules. Its unique structure and functional groups make it a versatile compound for the development of new organic compounds with potential applications in various industries, including pharmaceuticals, materials science, and agrochemicals.
Check Digit Verification of cas no
The CAS Registry Mumber 21959-36-4 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,1,9,5 and 9 respectively; the second part has 2 digits, 3 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 21959-36:
(7*2)+(6*1)+(5*9)+(4*5)+(3*9)+(2*3)+(1*6)=124
124 % 10 = 4
So 21959-36-4 is a valid CAS Registry Number.
InChI:InChI=1/C13H15I2NO4/c1-3-20-13(19)11(16-7(2)17)6-8-4-9(14)12(18)10(15)5-8/h4-5,11,18H,3,6H2,1-2H3,(H,16,17)
21959-36-4Relevant articles and documents
Free-Radical Membrane Protein Footprinting by Photolysis of Perfluoroisopropyl Iodide Partitioned to Detergent Micelle by Sonication
Cheng, Ming,Guo, Chunyang,Li, Weikai,Gross, Michael L.
supporting information, p. 8867 - 8873 (2021/03/16)
A free-radical footprinting approach is described for integral membrane protein (IMP) that extends, significantly, the “fast photochemical oxidation of proteins” (FPOP) platform. This new approach exploits highly hydrophobic perfluoroisopropyl iodide (PFIPI) together with tip sonication to ensure efficient transport into the micelle interior, allowing laser dissociation and footprinting of the transmembrane domains. In contrast to water soluble footprinters, PFIPI footprints both the hydrophobic intramembrane and the hydrophilic extramembrane domains of the IMP vitamin K epoxide reductase (VKOR). The footprinting is fast, giving high coverage for Tyr (100 %) and Trp. The incorporation of the reagent with sonication does not significantly affect VKOR's enzymatic function, and tyrosine iodination does not compromise protease digestion and the subsequent analysis. The locations for the modifications are largely consistent with the corresponding solvent accessibilities, recommending this approach for future membrane protein footprinting.
