111276-71-2 Usage
Uses
Used in Biological Research:
L-Glutamic acid, N-(1-oxodecyl)is used as a research tool for studying the interactions between neurotransmitters and lipid membranes. Its hydrophobic properties enable it to bind to cellular membranes, providing insights into the mechanisms of neurotransmission and membrane dynamics.
Used in Pharmaceutical Development:
L-Glutamic acid, N-(1-oxodecyl)has potential applications in the development of novel therapeutic agents. Its unique structure and ability to interact with lipid membranes may be leveraged to design drugs targeting specific cellular pathways or receptors involved in various diseases.
Used in Drug Delivery Systems:
L-Glutamic acid, N-(1-oxodecyl)can be utilized in the design of drug delivery systems to improve the bioavailability and targeting of therapeutic agents. Its hydrophobic nature may facilitate the encapsulation of hydrophobic drugs, enhancing their solubility and stability in biological systems.
Used in Neurodegenerative Disease Research:
Given its structural similarity to L-glutamic acid, a neurotransmitter involved in various neurological processes, L-Glutamic acid, N-(1-oxodecyl)may be used in research aimed at understanding the role of glutamate in neurodegenerative diseases such as Alzheimer's and Parkinson's. Its hydrophobic properties could provide insights into the mechanisms of glutamate-mediated neuronal toxicity and potential therapeutic interventions.
Check Digit Verification of cas no
The CAS Registry Mumber 111276-71-2 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,1,1,2,7 and 6 respectively; the second part has 2 digits, 7 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 111276-71:
(8*1)+(7*1)+(6*1)+(5*2)+(4*7)+(3*6)+(2*7)+(1*1)=92
92 % 10 = 2
So 111276-71-2 is a valid CAS Registry Number.
111276-71-2Relevant academic research and scientific papers
Wipf, Peter,Cunningham, April,Rice, Robert L.,Lazo, John S.
, p. 165 - 177 (1997)
In eukaryotes, phosphorylation of serine, threonine, and tyrosine residues on proteins is a fundamental posttranslational regulatory process for such functions as signal transduction, gene transcription, RNA splicing, cellular adhesion, apoptosis, and cell cycle control. Based on functional groups present in natural product serine/threonine protein phosphatase (PSTPase) inhibitors, we have designed pharmacophore model 1 and demonstrated the feasibility of a combinatorial chemistry approach for the preparation of functional analogues of 1. Preliminary biological testing of 18 structural variants of 1 has identified two compounds with growth inhibitory activity against cultured human breast cancer cells. In vitro inhibition of the PSTPase PP2A was demonstrated with compound Id. Using flow cytometry we observed that compound If caused prominent inhibition in the G1 phase of the cell cycle. Thus, the combinatorial modifications of the minimal pharmacophore 1 can generate biologically interesting antiproliferative agents.
