6610-36-2

Basic information

• Product Name: 4-(4-CHLOROBENZYL)-3-THIOSEMICARBAZIDE
• Synonyms: 4-(4-CHLOROBENZYL)-3-THIOSEMICARBAZIDE;4-(4-CHLOROBENZYL)-THIOSEMICARBAZIDE
• CAS NO: 6610-36-2
• Molecular Formula: C₈H₁₀ClN₃S
• Molecular Weight: 215.7
• Mol File: 6610-36-2.mol
• Article Data: 5

Chemical Properties

• Melting Point: 174-175°C
• Boiling Point: °Cat760mmHg
• Flash Point: °C
• Appearance: /
• Density: 1.371g/cm³
• Refractive Index: 1.731
• CAS DataBase Reference: 4-(4-CHLOROBENZYL)-3-THIOSEMICARBAZIDE(CAS DataBase Reference)
• NIST Chemistry Reference: 4-(4-CHLOROBENZYL)-3-THIOSEMICARBAZIDE(6610-36-2)
• EPA Substance Registry System: 4-(4-CHLOROBENZYL)-3-THIOSEMICARBAZIDE(6610-36-2)

Safety Data

• Statements: 23/24/25
• Safety Statements: 26-36/37/39
• RIDADR: 2811
• HazardClass: IRRITANT
• Hazardous Substances Data: 6610-36-2(Hazardous Substances Data)

Usage

General Description

4-(4-Chlorobenzyl)-3-thiosemicarbazide is a chemical compound with the molecular formula C9H10ClN3S. It is a derivative of thiosemicarbazide, which is a versatile building block in organic synthesis due to its ability to form various heterocycles and metal complexes. The presence of a chlorine atom and a benzyl group in its structure makes 4-(4-Chlorobenzyl)-3-thiosemicarbazide a potentially useful compound in medicinal chemistry, as it may exhibit biological activities such as antimicrobial, antiviral, and anticancer properties. Furthermore, thiosemicarbazides have been studied for their potential as chelating agents, and derivatives like 4-(4-Chlorobenzyl)-3-thiosemicarbazide could be valuable in the development of new coordination compounds for various applications in chemistry and materials science.

InChI:InChI=1/C26H20N4O3S/c1-15-18(25-29-23-21(33-25)11-6-12-27-23)9-5-10-20(15)28-26(34)30-24(31)19-13-16-7-3-4-8-17(16)14-22(19)32-2/h3-14H,1-2H3,(H2,28,30,31,34)

Upstream product

• 104-86-9 4-chlorobenzylamine 
• 3694-45-9 4-chlorobenzylisothiocyanate 
• 75-15-0 carbon disulfide 

Downstream Products

• 1298017-06-7 C₂₀H₁₇ClN₄O₂S 
• 34930-27-3 (4-chloro-benzyl)-[1,2,3,4]thiatriazol-5-yl-amine 

Relevant articles and documents

Structural revision of the Mcl-1 inhibitor MIM1: synthesis and biological studies on ovarian cancer cells with evaluation of designed analogues

In the area of cancer research, the development of new and potent inhibitors of anti-apoptotic proteins is a very active and promising topic. The small molecule MIM1 has been reported earlier as one of the first selective inhibitors of the anti-apoptotic protein Mcl-1. In the present paper, we first revised the structure of this molecule based on extensive physicochemical analyses. Then we designed and synthesized a focused library of analogues for the corrected structure of MIM1. Next, these molecules were subjected to a panel ofin cellulobiological studies, allowing the identification of dual Bcl-xL/Mcl-1 inhibitors, as well as selective Mcl-1 inhibitors. These results have been complemented by fluorescence polarization assays with the Mcl-1 protein. Preliminary structure-activity relationships were discussed and extensive molecular modelling studies allowed us to propose a rationale for the biological activity of this series of new inhibitors, in particular for the selectivity of inhibition of Mcl-1versusBcl-xL

Synthesis, crystal structure, molecular docking studies and bio-evaluation of some N4-benzyl-substituted isatin-3-thiosemicarbazones as urease and glycation inhibitors

Fifteen N4-benzyl-substituted isatin-3-thiosemicarbazones 5a-o were synthesized and evaluated for their urease and glycation inhibitory potential. Lemna aequinocitalis growth and Artemia salina assays were also done to determine their phytotoxi

Synthesis, X-ray molecular structure, biological evaluation and molecular docking studies of some N4-benzyl substituted 5-nitroisatin-3-thiosemicarbazones

A series of fifteen N4-benzyl substituted 5-nitroisatin-3-thiosemicarbazones 5a–o was synthesized and evaluated for urease inhibitory, phytotoxic and cytotoxic influences. All the compounds proved to be highly potent inhibitors of the enzyme, s