7780-14-5 Usage
Uses
Used in Organic Chemistry:
4-Nitrophenyl caproate is used as a reagent for the synthesis of other organic compounds, particularly for the production of ester derivatives. Its ability to undergo esterification reactions makes it a valuable component in the creation of a diverse range of chemical products.
Used in Research and Development:
In the realm of research and development, 4-Nitrophenyl caproate is utilized for its distinctive chemical properties. It is explored for potential applications in medicinal and pharmaceutical chemistry, where its reactivity and structural features may contribute to the discovery of new drugs or therapeutic agents.
Used in Medicinal Chemistry:
4-Nitrophenyl caproate is employed as a building block in the design and synthesis of pharmaceutical compounds. Its presence in a molecule can influence the pharmacokinetics and pharmacodynamics of drug candidates, potentially enhancing their efficacy and safety profiles.
Used in Pharmaceutical Chemistry:
In pharmaceutical chemistry, 4-Nitrophenyl caproate is used to develop prodrugs or drug delivery systems. Its reactivity can be harnessed to create compounds that are converted into active pharmaceutical ingredients within the body, thereby improving drug absorption, distribution, and targeting.
Check Digit Verification of cas no
The CAS Registry Mumber 7780-14-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,7,8 and 0 respectively; the second part has 2 digits, 1 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 7780-14:
(6*7)+(5*7)+(4*8)+(3*0)+(2*1)+(1*4)=115
115 % 10 = 5
So 7780-14-5 is a valid CAS Registry Number.
7780-14-5Relevant academic research and scientific papers
Hu, Lan,Zhao, Yan
, p. 5580 - 5584 (2018)
A difficult challenge in synthetic enzymes is the creation of substrate-selective active sites with accurately positioned catalytic groups. Covalent molecular imprinting in cross-linked micelles afforded such active sites in protein-sized, water-soluble nanoparticle catalysts. Our method allowed a systematic tuning of the distance of the catalytic group to the bound substrate. The catalysts displayed enzyme-like kinetics and easily distinguished substrates with subtle structural differences.
