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Related Concept Videos

Oral Hypoglycemic Agents: α-Glucosidase Inhibitors01:19

Oral Hypoglycemic Agents: α-Glucosidase Inhibitors

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α-glucosidase inhibitors, including acarbose (Precose), miglitol (Glyset), and voglibose (Voglib) (primarily available in Asia), are drugs that control blood sugar levels by delaying the digestion of starch and disaccharides. They achieve this by inhibiting α-glucosidase enzymes in the intestine, which slow the absorption of carbohydrates in the intestine, which in turn leads to a prolonged release of the glucoregulatory hormone GLP-1 from intestinal L-cells.
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α-Alkylation of Ketones via Enolate Ions01:10

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Ketones with α protons are deprotonated by strong bases like lithium diisopropylamide (LDA) to form enolate ions. The anion is stabilized by resonance, and its hybrid structure exhibits negative charges on the carbonyl oxygen and the α carbon. This ambident nucleophile can attack an electrophile via two possible sites: the carbonyl oxygen, known as O-attack, or the α carbon, known as C-attack. The nucleophilic attack via the carbanionic site is preferred. This is due to the...
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Factors Affecting α-Alkylation of Ketones: Choice of Base01:10

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α-Alkylation of ketones is achieved in the presence of alkyl halides and a base. The reaction proceeds via the formation of an enolate ion followed by nucleophilic substitution. The choice of base employed is essential as it is the key factor in determining the reaction outcome.
The reaction involving bases like EtO− whose conjugate acid EtOH (pKa = 15.9) is stronger than the ketone (pKa = 19.2) results in an equilibrium mixture with higher ketone concentration. As a consequence,...
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Predator-Prey Interactions02:39

Predator-Prey Interactions

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Predators consume prey for energy. Predators that acquire prey and prey that avoid predation both increase their chances of survival and reproduction (i.e., fitness). Routine predator-prey interactions elicit mutual adaptations that improve predator offenses, such as claws, teeth, and speed, as well as prey defenses, including crypsis, aposematism, and mimicry. Thus, predator-prey interactions resemble an evolutionary arms race.
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Nucleophilic substitution in α-halocarbonyl compounds can be achieved via an SN2 pathway. The reaction in α-haloketones is generally carried out with less basic nucleophiles. The use of strong basic nucleophiles leads to the generation of α-haloenolate ions, which often participate in other side reactions.
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By replacing an α-hydrogen with a halogen, acid-catalyzed α-halogenation of aldehydes or ketones yields a monohalogenated product
In the first step of the mechanism, the acid protonates the carbonyl oxygen resulting in a resonance-stabilized cation, which subsequently loses an α-hydrogen to form an enol tautomer. The C=C bond in an enol is highly nucleophilic because of the electron-donating nature of the –OH group. Consequently, the double bond attacks an electrophilic halogen to form a...
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Visualisation and Quantification of Intracellular Interactions of Neisseria meningitidis and Human α-actinin by Confocal Imaging
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[Interaction between gomizine D and α-glucosidase].

Hui Zhang1, Yuan-Yuan Wu1, Chen-Ye Huang1

  • 1College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou 310014, China.

Zhongguo Zhong Yao Za Zhi = Zhongguo Zhongyao Zazhi = China Journal of Chinese Materia Medica
|January 30, 2018
PubMed
Summary

Gomizine D effectively inhibits alpha-glucosidase, showing greater potency than acarbose. This natural compound offers a promising avenue for developing new alpha-glucosidase inhibitors.

Keywords:
gomizine Dinhibition rateinteractionmolecular dockingα-glucosidase

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Area of Science:

  • Biochemistry
  • Enzyme Inhibition
  • Pharmacology

Background:

  • Alpha-glucosidase plays a crucial role in carbohydrate digestion.
  • Inhibiting alpha-glucosidase is a therapeutic strategy for managing diabetes.
  • Gomizine D is a compound with potential biological activities.

Purpose of the Study:

  • To investigate the inhibitory effect of gomizine D on alpha-glucosidase.
  • To determine the kinetic parameters and binding mode of gomizine D interaction with alpha-glucosidase.

Main Methods:

  • Enzyme inhibition assays using p-nitrophenyl-α-D-glucopyranoside (PNPG) substrate.
  • Determination of IC50 and Ki values.
  • Molecular docking simulations using AutoDock Vina.
  • UV spectroscopy to analyze changes in enzyme structure.

Main Results:

  • Gomizine D exhibited a lower IC50 value (0.59 mmol•L⁻¹) compared to acarbose (1.95 mmol•L⁻¹).
  • Gomizine D acts as a reversible, non-competitive inhibitor with a Ki of 4.026 g•L⁻¹.
  • Molecular docking revealed a lower binding energy for gomizine D (-7.7 kcal•mol⁻¹) than acarbose (-6.6 kcal•mol⁻¹).
  • UV spectroscopy indicated alterations in the microenvironment and reduced polarity of alpha-glucosidase upon binding with gomizine D.

Conclusions:

  • Gomizine D is a potent inhibitor of alpha-glucosidase.
  • The findings suggest gomizine D has a favorable binding interaction with alpha-glucosidase.
  • Gomizine D represents a potential therapeutic candidate for alpha-glucosidase-related conditions.