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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

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Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
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¹³C NMR: ¹H–¹³C Decoupling01:04

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The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
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In Vitro Drug Dissolution: Alternative Methods01:17

In Vitro Drug Dissolution: Alternative Methods

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Alternative drug dissolution methods include the rotating bottle, intrinsic dissolution test, peristalsis, and the Franz diffusion cell method. The rotating bottle method involves meticulously rotating tightly capped controlled-release beads in a temperature-controlled bath. Periodic decanting of samples allows for residue assay, followed by refilling with fresh medium and testing at various pH levels to emulate the gastrointestinal tract conditions.In contrast, the intrinsic dissolution test...
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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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Theories of Dissolution: Diffusion Layer Model01:15

Theories of Dissolution: Diffusion Layer Model

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Dissolution, the process by which drug particles dissolve in a solvent, is explained by the diffusion layer model, a theoretical framework that simulates the absorption of oral drugs and allows us to analyze experimental data.
This process starts with a thin layer, saturated with the drug, forming at the interface between the solid and liquid. The solute then diffuses from this layer into the main solution. The Noyes-Whitney equation suggests that the rate of dissolution relies on the diffusion...
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Factors Affecting Dissolution: Polymorphism, Amorphism and Pseudopolymorphism01:21

Factors Affecting Dissolution: Polymorphism, Amorphism and Pseudopolymorphism

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Polymorphism refers to the existence of a drug substance in multiple crystalline forms, known as polymorphs. Recently, this term has been expanded to include solvates (forms containing a solvent), amorphous forms (non-crystalline forms), and desolvated solvates (forms from which the solvent has been removed).
Some polymorphic crystals possess lower aqueous solubility than their amorphous counterparts, leading to incomplete absorption. For instance, the oral suspension of Chloramphenicol, which...
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Dissolution Dynamic Nuclear Polarization Instrumentation for Real-time Enzymatic Reaction Rate Measurements by NMR
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Applications of Dissolution-DNP for NMR Screening.

Yaewon Kim1, Christian Hilty1

  • 1Chemistry Department, Texas A&M University, College Station, TX, United States.

Methods in Enzymology
|January 15, 2019
PubMed
Summary

Dissolution dynamic nuclear polarization (D-DNP) significantly enhances Nuclear Magnetic Resonance (NMR) sensitivity for screening protein-ligand interactions. This advanced NMR technique improves drug discovery efficiency by enabling faster, more accurate binding affinity and structural analyses.

Keywords:
Dissolution dynamic nuclear polarizationDrug discoveryFlow-NMRLigand-based screeningProtein–ligand interactionsRelaxometry

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Drug Discovery

Background:

  • Protein-ligand interactions are crucial in drug discovery, traditionally assessed using Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Standard NMR suffers from low sensitivity, requiring high concentrations of biomolecules and ligands.
  • Hyperpolarization techniques, particularly dissolution dynamic nuclear polarization (D-DNP), offer a substantial increase in NMR signal sensitivity.

Purpose of the Study:

  • To introduce basic techniques for applying D-DNP to screening protein-ligand interactions.
  • To demonstrate how D-DNP-enhanced NMR can determine binding affinities, structural, and dynamic parameters.
  • To explore methods for efficient screening and structural information acquisition in drug discovery.

Main Methods:

  • Brief review of hyperpolarization procedures for D-DNP.
  • Description of NMR detection methods focusing on chemical shift and relaxation parameter changes.
  • Application of competitive binding experiments with known ligands for affinity and pharmacophore analysis.

Main Results:

  • D-DNP significantly boosts NMR signal sensitivity, enabling detection at lower concentrations and near-stoichiometric conditions.
  • NMR methods utilizing D-DNP can accurately measure binding affinities and provide structural insights.
  • Solutions for challenges with non-renewable hyperpolarization, such as multiplexed NMR detection, are presented.

Conclusions:

  • D-DNP-enhanced NMR provides a powerful toolkit for efficient screening of protein-ligand interactions.
  • The substantial signal enhancement facilitates the detection of binding affinity, structure, and dynamics.
  • This approach holds significant potential for accelerating drug discovery pipelines.