125161-50-4

Basic information

• Product Name: 1,2,3,4,6-penta-O-butanoyl-alpha-D-galactopyranose
• CAS NO: 125161-50-4
• Molecular Formula: C₂₆H₄₂O₁₁
• Molecular Weight: 530.6051
• Mol File: 125161-50-4.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 557.2°C at 760 mmHg
• Flash Point: 231.9°C
• Density: 1.15g/cm³
• Vapor Pressure: 1.89E-12mmHg at 25°C
• Refractive Index: 1.483
• CAS DataBase Reference: 1,2,3,4,6-penta-O-butanoyl-alpha-D-galactopyranose(CAS DataBase Reference)
• NIST Chemistry Reference: 1,2,3,4,6-penta-O-butanoyl-alpha-D-galactopyranose(125161-50-4)
• EPA Substance Registry System: 1,2,3,4,6-penta-O-butanoyl-alpha-D-galactopyranose(125161-50-4)

Safety Data

• Hazardous Substances Data: 125161-50-4(Hazardous Substances Data)

Usage

General Description

1,2,3,4,6-penta-O-butanoyl-alpha-D-galactopyranose is a chemical compound with a complex molecular structure. It is a derivative of alpha-D-galactopyranose, a type of sugar molecule. The compound is formed by attaching five butanoyl groups to the hydroxyl (OH) groups on the galactopyranose ring. This modification results in the formation of a molecule with multiple acyl groups, making it more hydrophobic and less soluble in water. This chemical modification can alter the properties and reactivity of the original sugar molecule, and it may have applications in various fields, such as pharmaceuticals, food industry, or material science.

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Relevant articles and documents

Design, synthesis, and biological evaluation of novel carbohydrate-based sulfamates as carbonic anhydrase inhibitors

Carbonic anhydrases (CAs) IX and XII are enzymes with newly validated potential for the development of personalized, first-in-class cancer chemotherapies. Here we present the design and synthesis of novel carbohydrate-based CA inhibitors, several of which were very efficient inhibitors (Ki10 nM) with good selectivity for cancer-associated CA isozymes over off-target CA isozymes. All inhibitors comprised a carbohydrate core with one hydroxyl group derivatized as a sulfamate. Five different carbohydrates were chosen to present a selection of molecular shapes with subtle stereochemical differences to the CA enzymes active site. Variable modifications of the remaining sugar hydroxyl groups were incorporated to provide an incremental coverage of chemical property parameters that are associated with biopharmaceutical performance. All sulfamate inhibitors displayed ligand efficiencies that are consistent with those reported for good drug lead candidates.