5391-65-1

Usage

Also known as

Octodrine

Chemical category

Amine

Psychoactive substance

Stimulant, similar to amphetamines and ephedrine

Uses

Energy supplements, weight loss products, performance-enhancing drug in sports and bodybuilding

Health risks

Potential health risks, lack of safety data

Regulatory status

Banned by various sports organizations and regulatory agencies, classified as a doping agent, not approved for human consumption in many countries

Availability

Still available on the market from some unregulated sources.

Upstream product

• 16751-58-9 3-aminohexane 
• 1421280-12-7 1-(3-azidohexyl)benzene 
• 1421280-11-6 1-phenylhexan-3-yl 4-methylbenzenesulfonate 
• 2180-43-0 1-phenyl-3-hexanol 
• 29898-25-7 1-phenylhexan-3-one 

Downstream Products

• 1421280-13-8 1-phenylhexan-3-amine 
• 1429325-14-3 C₁₈H₂₈N₂O 
• 1421366-98-4 (2S)-1-(2-oxo-2-phenylacetyl)-N-(1-phenylhexan-3-yl)piperidine-2-carboxamide 
• 4812-67-3 (Z)-3-(1-Phenethyl-butylcarbamoyl)-acrylic acid 

Relevant academic research and scientific papers

Catalytic C(sp3)?H Arylation of Free Primary Amines with an exo Directing Group Generated In Situ

Herein, we report the palladium-catalyzed direct arylation of unactivated aliphatic C?H bonds in free primary amines. This method takes advantage of an exo-imine-type directing group (DG) that can be generated and removed in situ. A range of unprotected aliphatic amines are suitable substrates, undergoing site-selective arylation at the γ-position. Methyl as well as cyclic and acyclic methylene groups can be activated. Furthermore, when aniline-derived substrates were used, preliminary success with δ-C?H arylation was achieved. The feasibility of using the DG component in a catalytic fashion was also demonstrated.

The precise chemical-physical nature of the pharmacore in FK506 binding protein inhibition: ElteX, a new class of nanomolar FKBP12 ligands

Due to its central role in immunosuppression and cell proliferation and due to its specific peptidyl-prolyl-isomerase (PPI) function, the FKBP protein family is at the crossroad of several important metabolic pathways. Members of this family, and notably FK506 binding protein (FKBP12), are thought to be involved in neurodegenerative diseases such as Alzheimer disease, Parkinson disease, multiple sclerosis, amyotrophic lateral sclerosis, as well as in proliferation disorders and cancer. Using an interdisciplinary approach based on computational, synthetic, and experimental techniques, we show that the best potential binders for FKBP proteins optimally expose the two contiguous carbonyl oxygen in the proline-mimetic chain for FKBP docking and are characterized by the abundance of rigid quasi-cyclic structures stabilized in aqueous solution by intraligand hydrophobic interactions mimicking the macrolide structure of the natural FKBP binders FK506 and Rapamycin. These peculiar structural and chemical-physical features define at the same time an ElteX compound and the minimal pharmacore in the FKBP family, shedding new light on the isomerization mechanism of the PPI domain. On the basis of the above hypothesis, we have successfully designed and synthesized several nanomolar ElteX FKBP12 ligands. Among these, ElteN378 is a new low atomic weight ligand with affinity comparable to that of the macrolide Rapamycin.