125161-50-4 Usage
Chemical compound
A complex molecule derived from alpha-D-galactopyranose, a type of sugar molecule.
Structure
Consists of a galactopyranose ring with five butanoyl groups attached to the hydroxyl (OH) groups.
Hydrophobicity
The attachment of butanoyl groups increases the hydrophobicity of the molecule, making it less soluble in water.
Reactivity
The chemical modification can alter the properties and reactivity of the original sugar molecule.
Applications
Potential uses in various fields, such as pharmaceuticals, food industry, or material science.
Derivative
A modified version of alpha-D-galactopyranose with additional acyl groups.
Stereochemistry
Retains the alpha-D configuration of the original galactopyranose molecule.
Functional groups
Contains ester linkages between the butanoyl groups and the hydroxyl groups of the galactopyranose ring.
Solubility
Less soluble in water due to the increased hydrophobicity from the butanoyl groups.
Check Digit Verification of cas no
The CAS Registry Mumber 125161-50-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,5,1,6 and 1 respectively; the second part has 2 digits, 5 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 125161-50:
(8*1)+(7*2)+(6*5)+(5*1)+(4*6)+(3*1)+(2*5)+(1*0)=94
94 % 10 = 4
So 125161-50-4 is a valid CAS Registry Number.
125161-50-4Relevant articles and documents
Design, synthesis, and biological evaluation of novel carbohydrate-based sulfamates as carbonic anhydrase inhibitors
Lopez, Marie,Trajkovic, Jonathan,Bornaghi, Laurent F.,Innocenti, Alessio,Vullo, Daniela,Supuran, Claudiu T.,Poulsen, Sally-Ann
supporting information; experimental part, p. 1481 - 1489 (2011/05/12)
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.