106873-99-8 Usage
Uses
Used in Degradable Polymers:
2-N-Formylamino-butyric acid is used as a component in degradable polymers for its ability to enhance the solubility and stability of these materials, making them more environmentally friendly and suitable for various applications.
Used in Food Packaging:
In the food packaging industry, 2-N-Formylamino-butyric acid is used as an additive to improve the packaging material's properties, such as its barrier to gases and moisture, and to extend the shelf life of packaged food products.
Used in Drug Delivery Systems:
2-N-Formylamino-butyric acid is employed in drug delivery systems to enhance the solubility and bioavailability of pharmaceutical compounds, improving the effectiveness and safety of drug administration.
Used in Biosensors:
2-N-FORMYLAMIONO-BUTYRICACID is used in the development of biosensors for its ability to interact with biological molecules, allowing for the detection and measurement of various biological substances.
Used in Coating Materials:
2-N-Formylamino-butyric acid is used as an ingredient in coating materials to improve their properties, such as adhesion, durability, and resistance to environmental factors, making them suitable for various applications, including industrial and consumer products.
Check Digit Verification of cas no
The CAS Registry Mumber 106873-99-8 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,0,6,8,7 and 3 respectively; the second part has 2 digits, 9 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 106873-99:
(8*1)+(7*0)+(6*6)+(5*8)+(4*7)+(3*3)+(2*9)+(1*9)=148
148 % 10 = 8
So 106873-99-8 is a valid CAS Registry Number.
106873-99-8Relevant academic research and scientific papers
Remote binding energy in antibody catalysis: Studies of a catalytically unoptimized specificity pocket
Wade, Herschel,Scanlan, Thomas S.
, p. 1434 - 1443 (2007/10/03)
Binding interactions remote from the hydrolytic reaction center have been probed with substrate and phosphonate transition state analogues to understand how these types of interactions are used to promote catalysis in the 17E8 system. We find that the hapten-generated recogniton pocket in 17E8 has properties that are analogous to those of specificity pockets in enzymes. We have also found that there are specific requirements to form catalytically productive interactions between the side chain and the recognition pocket including conformation, size, and geometry. An additional requirement includes favorable simultaneous interactions between the side chain and binding pocket along with favorable interactions with the oxyanion hole. The 17E8 side chain recognition pocket seems to be less catalytically efficient than analogous pockets in enzymatic systems. The apparent binding energy gained from the methylene-pocket interactions in the 17E8 system is significantly smaller than those observed in natural enzymes. Furthermore, 17E8 does not use specific interactions in the recognition pocket to significantly affect catalytic turnover (kcat) which is thought to be a trait of an unoptimized catalyst. Analysis of the crystal structure of the 17E8·hapten complex has allowed for the identification of differences between the active sites of 17E8 and several proteases. The identified differences give insight to the sources of the inefficient use of binding energy.
