70696-37-6

Basic information

• Product Name: N-[(5-CHLOROTHIEN-2-YL)METHYL]-N-METHYLAMINE
• Synonyms: 1-(5-chlorothiophen-2-yl)-N-methylmethanamine
• CAS NO: 70696-37-6
• Molecular Formula: C₆H₈ClNS
• Molecular Weight: 162.6598
• Mol File: 70696-37-6.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 199 °C at 760 mmHg
• Flash Point: 74.2 °C
• Appearance: /
• Vapor Pressure: 0.349mmHg at 25°C
• CAS DataBase Reference: N-[(5-CHLOROTHIEN-2-YL)METHYL]-N-METHYLAMINE(CAS DataBase Reference)
• NIST Chemistry Reference: N-[(5-CHLOROTHIEN-2-YL)METHYL]-N-METHYLAMINE(70696-37-6)
• EPA Substance Registry System: N-[(5-CHLOROTHIEN-2-YL)METHYL]-N-METHYLAMINE(70696-37-6)

Safety Data

• Hazardous Substances Data: 70696-37-6(Hazardous Substances Data)

Usage

Uses

(5-Chlorothiophen-2-ylmethyl)-methyl-amine

InChI:InChI=1/C6H8ClNS/c1-8-4-5-2-3-6(7)9-5/h2-3,8H,4H2,1H3/p+1

Upstream product

• 7283-96-7 5-Chloro-2-thiophenecarboxaldehyde 

Downstream Products

• 70696-38-7 2-Chloro-4-phenyl-6-methyl-4,5,6,7-tetrahydro-thieno[2,3-c]pyridine hydrochloride 
• 775535-81-4 1-(4-Bromo-phenyl)-2-[(5-chloro-thiophen-2-ylmethyl)-methyl-amino]-ethanol 
• 734492-75-2 2-[(5-Chloro-thiophen-2-ylmethyl)-methyl-amino]-1-p-tolyl-ethanol 
• 777810-34-1 2-[(5-Chloro-thiophen-2-ylmethyl)-methyl-amino]-1-phenyl-ethanol 
• 70696-53-6 4-(4-bromo-phenyl)-2-chloro-6-methyl-4,5,6,7-tetrahydro-thieno[2,3-c]pyridine 
• 70696-55-8 2-chloro-4-(4-chloro-phenyl)-6-methyl-4,5,6,7-tetrahydro-thieno[2,3-c]pyridine 
• 90553-56-3 2-chloro-6-methyl-4-p-tolyl-4,5,6,7-tetrahydro-thieno[2,3-c]pyridine 
• 90553-49-4 2-chloro-6-methyl-4-phenyl-4,5,6,7-tetrahydro-thieno[2,3-c]pyridine 
• 107445-13-6 1-(4-chlorophenyl)-2-<<(5-chloro-2-thienyl)methyl>methylamino>ethanol 

Relevant articles and documents

Hydantoin analogs inhibit the fully assembled ClpXP protease without affecting the individual peptidase and chaperone domains

Proteolysis mediated by ClpXP is a crucial cellular process linked to bacterial pathogenesis. The development of specific inhibitors has largely focused on ClpP. However, this focus was challenged by a recent finding showing that conformational control by ClpX leads to a rejection of ClpP binders. Thus, we here follow up on a hit molecule from a high throughput screen performed against the whole ClpXP complex and demonstrate that stable inhibition with high potency is possible. Further investigations revealed that the small molecule binds to ClpP without affecting its activity. Likewise, the molecule does not inhibit ClpX and retains the overall oligomeric state of ClpXP upon binding. Structure activity relationship studies confirmed structural constraints in all three parts of the molecule suggesting binding into a defined stereospecific pocket. Overall, the inhibition of ClpXP without affecting the individual components represents a novel mechanism with perspectives for further optimization for in situ applications.