125772-42-1

Basic information

• Product Name: 4-TERT-BUTYL-BENZAMIDINE
• Synonyms: 4-TERT-BUTYL-BENZAMIDINE;4-ISOPROPYLBENZENECARBOXIMIDAMIDE;BenzenecarboxiMidaMide, 4-(1,1-diMethylethyl)-;4-(tert-butyl)benzimidamide
• CAS NO: 125772-42-1
• Molecular Formula: C11H16N2
• Molecular Weight: 176.26
• Product Categories: pharmacetical
• Mol File: 125772-42-1.mol

Chemical Properties

• Boiling Point: 260.6°C at 760 mmHg
• Flash Point: 111.4°C
• Appearance: /
• Density: 0.99g/cm³
• Vapor Pressure: 0.0121mmHg at 25°C
• Refractive Index: 1.526
• CAS DataBase Reference: 4-TERT-BUTYL-BENZAMIDINE(CAS DataBase Reference)
• NIST Chemistry Reference: 4-TERT-BUTYL-BENZAMIDINE(125772-42-1)
• EPA Substance Registry System: 4-TERT-BUTYL-BENZAMIDINE(125772-42-1)

Safety Data

• Hazardous Substances Data: 125772-42-1(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Research and Drug Discovery:
4-TERT-BUTYL-BENZAMIDINE is used as a reagent in pharmaceutical research and drug discovery for its ability to inhibit serine proteases, which are crucial enzymes in various biological processes. Its steric hindrance and stability make it a valuable tool in the development of new drugs targeting these enzymes.
Used in Chemical Synthesis:
In the field of chemical synthesis, 4-TERT-BUTYL-BENZAMIDINE is used as a building block for the creation of more complex organic compounds. Its stability and reactivity with other molecules facilitate the synthesis of a variety of organic compounds for various applications.
Used in Enzyme Inhibition Studies:
4-TERT-BUTYL-BENZAMIDINE is employed as an inhibitor in enzyme inhibition studies, particularly for serine proteases. Its potent and selective inhibition properties make it an ideal candidate for understanding the mechanisms of these enzymes and their role in disease processes.
Used in Organic Chemistry Research:
In the realm of organic chemistry research, 4-TERT-BUTYL-BENZAMIDINE is used as a model compound to study the effects of steric hindrance and stability on chemical reactions. Its unique properties allow researchers to explore new reaction pathways and develop innovative synthetic methods.

InChI:InChI=1/C11H16N2/c1-11(2,3)9-6-4-8(5-7-9)10(12)13/h4-7H,1-3H3,(H3,12,13)

Upstream product

• 4210-32-6 4-tert-butyl benzonitrile 

Downstream Products

• 945212-41-9 2-(4-tert-butylphenyl)-4,6-dihydroxypyrimidine 

Relevant articles and documents

MACROCYCLIC BROAD SPECTRUM ANTIBIOTICS

Provided herein are antibacterial compounds, wherein the compounds in some embodiments have broad spectrum bioactivity. In various embodiments, the compounds act by inhibition of bacterial type 1 signal peptidases SpsB and/or LepB, an essential protein in bacteria. Pharmaceutical compositions and methods for treatment using the compounds described herein are also provided.

MACROCYCLIC BROAD SPECTRUM ANTIBIOTICS

Provided herein are antibacterial compounds, wherein the compounds in some embodiments have broad spectrum bioactivity. In various embodiments, the compounds act by inhibition of bacterial type 1 signal peptidase (SpsB), an essential protein in bacteria. Pharmaceutical compositions and methods for treatment using the compounds described herein are also provided.

Three distinct read-out modes for enzyme activity can operate in a semi-wet supramolecular hydrogel

Assays of hydrolytic enzyme activity, such as of glycosidases and phosphatase, as well as several proteases, using a semi-wet supramolecular hydrogel array composed of a glycosylated amino acetate are described. It has been demonstrated that the microcavity formed by gel fibrils is suitable to immobilize native enzymes without denaturation under semi-wet conditions, and thus the nanofiber has been rationally used as a sensing domain to monitor enzymatic reactions. By using a fluorogenic substrate, reducing the size of the hydrogel can significantly improve the problem of suppressed diffusion within the gel matrix thus making the hydrogel a promising semi-wet matrix for evaluating enzyme activity. Confocal laser scanning microscopy observa lions have shown that an environmentally sensitive fluorescent probe accumulates in the hydrophobic domain of the gel fiber and emits fluorescence more strongly upon hydrolytic cleavage of the substrate peptides. Not only a simple environmentally sensitive probe but also a FRET (fluorescence resonance energy transfer)-type read-out mode can be devised to analyze the enzymatic hydrolysis-triggered redistribution of the probe between the nano-space and the nanofiber to accomplish a more clearly distinguished enzyme assay. Thus, it is clear that three distinct read-out modes, that is, 1) fluorogenic substrates, 2) substrates bearing an environmentally sensitive probe, or 3) a substrate exhibiting FRET, can operate under the semi-wet hydrogel conditions used in these investigations. In addition, owing to the unique properties of the present supramolecular hydrogel in semi-wet conditions, that is, its phase-segregation properties and dynamics, the supramolecular substrate/enzyme array has successfully been used for high-throughput screening of single and multiple enzymes based on their activity, lysate analysis, and quantitative evaluation of inhibitor potency and selectivity.