24088-97-9

Usage

InChI:InChI=1/C8H13Cl/c1-2-3-4-5-6-7-8-9/h1H,3-8H2

Upstream product

• 34683-73-3 1-chloro-6-iodohexane 
• 1066-26-8 sodium acetylide 
• 6294-17-3 1-bromo-6-chlorohexane 
• 74-86-2 acetylene 
• 126232-81-3 8-chloro-1-(trimethylsilyl)-1-octyne 
• 629-11-8 1,6-hexanediol 
• 2163-00-0 1,6-dichlorohexane 
• 2009-83-8 6-chloro-1-hexanol 

Downstream Products

• 42513-36-0 1-chloro-7-dodecyne 
• 95159-06-1 16-Chlor-1-phenylhexadeca-6,9-diin 
• 871-90-9 8-chloro-oct-1-ene 
• 141493-81-4 2-bromo-8-chlorooct-1-ene 
• 98814-47-2 16-chlorohexadeca-6,9-diyne 
• 14959-86-5 (Z)-7-dodecenyl acetate 
• 16974-10-0 1-acetoxy-(Z)-7-tetradecene 
• 42513-39-3 12-chloro-dodec-5c-ene 
• 18325-59-2 sterculynic acid 
• 23144-52-7 8-chlorooctan-1-ol 
• 1642-49-5 dec-9-ynoic acid 
• 2012-14-8 9,12-octadecadiynoic acid 
• 38681-47-9 trans-Octadec-9-en-12-in-1-saeure 

Relevant academic research and scientific papers

FATTY ACID COMPOUND, PREPARATION METHOD THEREFOR AND USE THEREFOR

The present invention relates to a class of fatty acid compounds, a preparation method thereof and use thereof. The fatty acid compounds have the structure of the formula I, which has the ability to activate APMK and inhibit the glucose output in mouse primary hepatocytes. The fatty acid compounds can be used in preparing a medicament for the treatment of obesity or diabetes.

Mechanistic investigations of the rhodium catalyzed propargylic CH activation

Previously we reported the redox-neutral atom economic rhodium catalyzed coupling of terminal alkynes with carboxylic acids using the DPEphos ligand. We herein present a thorough mechanistic investigation applying various spectroscopic and spectrometric m

In situ selection of lead compounds by click chemistry: Target-guided optimization of acetylcholinesterase inhibitors

The target-guided, in situ click chemistry approach to lead discovery has been successfully employed for discovering acetylcholinesterase (AChE) inhibitors by incubating a selected enzyme/tacrine azide combination with a variety of acetylene reagents that were not previously known to interact with the enzyme's peripheral binding site. The triazole products, formed by the enzyme, were identified by HPLC-mass spectrometry analysis of the crude reaction mixtures. The target-guided lead discovery search was also successful when performed with reagent mixtures containing up to 10 components. From 23 acetylene reagents, the enzyme selected two phenyltetrahydroisoquinoline (PIQ) building blocks that combined with the tacrine azide within the active center gorge to form multivalent inhibitors that simultaneously associate with the active and peripheral binding sites. These new inhibitors are up to 3 times as potent as our previous phenylphenanthridinium-derived compounds, and with dissociation constants as low as 33 femtomolar, they are the most potent noncovalent AChE inhibitors known. In addition, the new compounds lack a permanent positive charge and aniline groups and possess fewer fused aromatic rings. Remarkably, despite the high binding affinity, the enzyme displayed a surprisingly low preference for one PIQ enantiomer over the other.

8,12-Dialkyl-PGE, and PGF1α

Prostaglandins E1 -type and F1 -type compounds of the formula EQU1 wherein R is hydrogen or a hydrocarbyl group containing from 1 to 12 carbon atoms, inclusive, wherein W is EQU2 or O =, wherein R7, R8, R9, R10, R11, R12, R13, and R14 are hydrogen or alkyl of 1 to 4 carbon atoms, inclusive, provided (1) that at least one of R7, R8, R9, R10, R11, R12, R13, and R14 is alkyl (2) that when R13 is alkyl, at least one of R7, R8, R9, R10, R11, R12, and R14 is alkyl, and (3) that when R7 is alkyl or thwn R7 and R8 are alkyl, at least one of R9, R10, R11, R12, R13, and R14 is alkyl; and the enantiomers and racemic mixtures thereof. These are useful for the same pharmacological purposes as the unsubstituted prostaglandins.