Topic
Aldose
About: Aldose is a research topic. Over the lifetime, 1270 publications have been published within this topic receiving 27197 citations. The topic is also known as: aldoses.
Papers published on a yearly basis
Papers
More filters
TL;DR: In this paper, the one pot conversion of 1,2,4,6-tetra-0,acetyl-β-D-glucopyranose, 1, into phenyl 2,4-6-tri-0-acetyl 3,0-trialkylsilyl-1,thio-β-,D-Glucopyanides, 3, is described.
31 citations
TL;DR: In this paper, a mixture of the β-d-septanose form and the acyclic form was found to be the dominant anomer of 2,3,4,5-Tetra-O -methyl-d -glucose.
30 citations
TL;DR: Aldose and aldehyde reductases are monomeric NADPH‐dependent oxidoreductases that catalyze the reduction of aldehydes and ketones to their corresponding alcohols, and the active site residues Tyr 50, His 113, and Trp 114 interacting with the hydrophilic heads of inhibitors are conserved.
Abstract: Aldose and aldehyde reductases are monomeric NADPH-dependent oxidoreductases that catalyze the reduction of a wide variety of aldehydes and ketones to their corresponding alcohols. The overall three-dimensional structures of the enzymes are composed of similar alpha/beta TIM-barrels, and the active site residues Tyr 50, His 113, and Trp 114 interacting with the hydrophilic heads of inhibitors are conserved. We have used molecular modeling and mass spectrometry to characterize the interactions between the enzymes and three aldose reductase inhibitors: tolrestat, sorbinil, and zopolrestat. Unlike the IC(50) values (concentration of inhibitor giving 50% of inhibition in solution), the Vc(50) values measured by mass spectrometry (accelerating voltage of ions needed to dissociate 50% of a noncovalent complex in the gas phase) for the two enzymes are similar, and they correlate with the electrostatic and hydrogen-bonding energies calculated between the conserved Tyr 50, His 113, and Trp 114 and the inhibitors. The results of our comparison agree with detailed structural information obtained by X-ray crystallography, suggesting that nonconserved residues from the C-terminal loop account for differences in IC(50) values for the two enzymes. Additionally, they confirm our previous assumption that the Vc(50) values reflect the enzyme-inhibitor electrostatic and hydrogen-bonding interactions and exclude the hydrophobic interactions.
30 citations
TL;DR: In this paper, the enantiomerically pure 1-(3-furyl)-1,2-dihydroxyethane derivatives 1 - (R), 2 -(R), 3 - (S) and 3 -(S) are described.
30 citations
TL;DR: The development of potent aldose reductase inhibitors as therapeutic agents for diabetic complications is highly desirable and the inhibitory action of 54 hydantoin derivatives consisting of 25 hydantoins, 21 2-thiohydantoins and 8 2-alkylthioHydantoins was tested on rat and bovine lens aldOSE reductases in vitro.
Abstract: The development of potent aldose reductase inhibitors as therapeutic agents for diabetic complications is highly desirable. The inhibitory action of 54 hydantoin derivatives consisting of 25 hydantoins, 21 2-thiohydantoins and 8 2-alkylthiohydantoins was therefore tested on rat and bovine lens aldose reductases in vitro. 1-(Phenylsulfonyl)-hydantoin (18) and its derivatives, 1-[(substituted phenyl) sulfonyl] hydantoins, were found to be potent inhibitors of the enzymes. 1-[(p-Bromophenyl) sulfonyl] hydantoin (49) was the most potent among them. It inhibited purified rat and bovine lens aldose reductases by 50% at 7×10-7M and 3.7×10-7M, respectively. Inhibition of rat and bovine lens aldose reductases by this compound (49) was due to its non-ionized form, but not the ionized form, and was of a non-competitive type with respect to DL-glyceraldehyde as a substrate.
30 citations