29147-98-6

Usage

Uses

Used in Biochemistry Research:
4-N-BUTYL-BENZAMIDINE HYDROCHLORIDE is used as a proteinase inhibitor for studying the mechanisms of enzyme action. Its ability to inhibit specific enzymes aids in understanding their roles in biological processes and disease pathways.
Used in Molecular Biology Research:
In molecular biology, 4-N-BUTYL-BENZAMIDINE HYDROCHLORIDE is utilized as a research tool to investigate the interactions between enzymes and their substrates or inhibitors, contributing to the discovery of novel therapeutic targets.
Used in Drug Development:
4-N-BUTYL-BENZAMIDINE HYDROCHLORIDE is used as a lead compound in the development of potential therapeutic agents. Its properties as a proteinase inhibitor make it a candidate for the treatment of conditions where enzyme activity is a factor.
Used in Enzyme Kinetics Studies:
4-N-BUTYL-BENZAMIDINE HYDROCHLORIDE is used as a reagent in experiments designed to study enzyme kinetics. Its solubility and inhibitory effects allow researchers to measure enzyme activity and understand the dynamics of enzymatic reactions.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, 4-N-BUTYL-BENZAMIDINE HYDROCHLORIDE is used as a starting material or intermediate in the synthesis of drugs targeting specific enzymes, potentially leading to treatments for various diseases.
Used in Diagnostic Applications:
4-N-BUTYL-BENZAMIDINE HYDROCHLORIDE may be employed in the development of diagnostic tools, where its interaction with enzymes can be leveraged to detect and monitor certain conditions or enzyme levels in biological samples.

Upstream product

• 20651-73-4 4-butylbenzonitrile 

Downstream Products

• 59855-59-3 2-(4-butyl-phenyl)-4-chloro-pyrimidine-5-carbonitrile 
• 59855-60-6 2-(4-butyl-phenyl)-6-oxo-1,6-dihydro-pyrimidine-5-carbonitrile 
• 74324-18-8 2-(4-Butyl-phenyl)-5-(4-pentyloxy-phenyl)-pyrimidine 
• 60202-97-3 2-<4-n-butyl-phenyl>-5-<4-n-butyloxy-phenyl>-pyrimidine 
• 81632-39-5 2-<4-Tolyl>-6-<4-butyl-phenylazo>-1,3-diaza-azulen 

Relevant academic research and scientific papers

Naphthyridine-based helical foldamers and macrocycles: Synthesis, cation binding, and supramolecular assemblies

(Figure Presented) Unraveling the factors that control the conformation of molecular chains is of great interest both for understanding the shape of biological molecular strands and for designing artificial ones that adopt desired forms. Thus, a variety of artificial folding codons have been identified that enforce the formation, among others, of helices, strands, and loops, the major emphasis being on the shape of the foldamer. We report herein the synthesis and study of a family of foldamers and macrocycles based on the 1,8-naphthyridine and pyrimidine units, whose internal cavity is large enough to accommodate ionic substrates, and focus on the impact of guest binding within a cylindrical environment. Interestingly, the binding event within these large oligomers is translated to the outside of the receptors and affects the interaction of the overall complexes with the outside world. For instance, alkali cations bind to the one-turn helices and macrocycles to promote fibril formation and aggregation. Also, polyammonium substrates are able to tune the length of the overall helix assemblies and the rigidity of long oligomers. The reported data on one-turn, two-turn helices and macrocycles not only allows one to devise a model for the ion-controlled supramolecular assembly of such systems but also provides evidence that such controlled scaffolds bear promise in the design of complex systems.

Understanding binding affinity: A combined isothermal titration calorimetry/molecular dynamics study of the binding of a series of hydrophobically modified benzamidinium chloride inhibitors to trypsin

The binding of a series of p-alkylbenzamidinium chloride inhibitors to the serine proteinase trypsin over a range of temperatures has been studied using isothermal titration (micro)calorimetry and molecular dynamics simulation techniques. The inhibitors h