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Related Concept Videos

Enzyme Inhibition01:30

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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Drug Discovery: Overview

Drug discovery is a multifaceted process involving extensive screening, testing, and optimization of lead compounds to identify potential new drugs for therapeutic use. It combines several approaches, including screening large numbers of natural products, chemical modification of known active molecules, identification of new drug targets, and rational design based on biological mechanisms and drug-receptor structure. These approaches are carried out in both academic research laboratories and...
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IR and UV–Vis Spectroscopy of Aldehydes and Ketones

Infrared spectroscopy, also known as vibrational spectroscopy, is mainly used to determine the types of bonds and functional groups in molecules. In aldehydes and ketones, the carbonyl (C=O) bond shows an absorption around 1710 cm-1. The C=O bond vibration of an aldehyde occurs at lower frequencies than that of a ketone. In addition to the C=O absorption in an aldehyde, the aldehydic C–H bond also gives two peaks in the 2700–2800 cm-1 range. This absorption, coupled with the C=O stretching, is...

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Identification of aldehyde dehydrogenase 1A1 modulators using virtual screening.

Vinayaka Kotraiah1, Diego Pallares, Deanna Toema

  • 1Exonhit Inc., Gaithersburg, MD, USA.

Journal of Enzyme Inhibition and Medicinal Chemistry
|March 3, 2012
PubMed
Summary

Parkinson's disease (PD) is linked to reduced ALDH1A1 enzyme activity. Alda-1, a compound, was found to activate ALDH1A1, offering a potential therapeutic avenue for PD by restoring toxic aldehyde metabolism.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Pharmacology

Background:

  • Aldehyde dehydrogenase (ALDH) isozymes ALDH1A1 and ALDH2 metabolize toxic biogenic aldehydes.
  • 3,4-dihydroxyphenylacetaldehyde (DOPAL) is a toxic aldehyde implicated in Parkinson's disease (PD).
  • ALDH1A1 mRNA is downregulated in the substantia nigra of human PD samples.

Purpose of the Study:

  • To investigate the role of ALDH1A1 in PD.
  • To identify compounds that can activate ALDH1A1.
  • To explore potential therapeutic strategies for PD.

Main Methods:

  • Genome-Wide SpliceArray (GWSA) technology to analyze ALDH1A1 mRNA levels.
  • DOPAL-induced ALDH1A1 inactivation assay.
  • Virtual screening of 19,943 compounds followed by in vitro testing.

Main Results:

  • ALDH1A1 mRNA was found to be downregulated in human PD substantia nigra tissue.
  • Alda-1, an ALDH2 activator, was also found to activate ALDH1A1.
  • Virtual screening identified one ALDH1A1 activator and two inhibitors.

Conclusions:

  • ALDH1A1 dysfunction may contribute to PD pathogenesis.
  • Alda-1 shows potential for activating ALDH1A1 and restoring DOPAL metabolism.
  • These findings provide a foundation for developing novel PD therapeutics targeting aldehyde metabolism.