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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

3.8K
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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Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

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Nuclear magnetic resonance (NMR) is a phenomenon exhibited by certain nuclei that can absorb characteristic radio frequency radiation under certain conditions. NMR has been extensively applied in molecular spectroscopy and medical diagnostic imaging. In both these applications, the molecule or subject under study is placed in a magnetic field and irradiated with radio frequency energy.
NMR spectroscopy generates a spectrum where the characteristic absorption frequencies of the sample are...
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Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

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The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse....
805
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

4.9K
Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.
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Identification and Quantification of Deranged Metabolites in Critically Ill Patients Using NMR-Based Metabolomics
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NMR spectroscopy as a characterization tool enabling biologics formulation development.

Junhe Ma1, Charles Pathirana1, David Q Liu2

  • 1Chemical Process Development, Bristol Myers Squibb Company, 1 Squibb Drive, New Brunswick, NJ 08903, United States.

Journal of Pharmaceutical and Biomedical Analysis
|October 29, 2022
PubMed
Summary

High-resolution nuclear magnetic resonance (NMR) spectroscopy, particularly the XL-ALSOFAST experiment, enhances the analysis of protein therapeutics in complex formulations. This advancement aids in developing stable biologic drugs by improving signal detection and reducing experimental time.

Keywords:
Biologics formulationHigher order structureNMR fingerprintingSolution NMRTherapeutic proteinsXL-ALSOFAST-HMQC

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Area of Science:

  • Biophysical characterization of protein therapeutics.
  • Advancements in analytical techniques for biopharmaceutical development.

Background:

  • Protein therapeutics can undergo conformational changes, leading to aggregation and degradation.
  • Current analytical methods struggle to assess protein integrity in complex formulations.
  • High-resolution nuclear magnetic resonance (NMR) spectroscopy offers a potential solution for specificity.

Purpose of the Study:

  • To highlight recent advancements in using NMR spectroscopy for biologics formulation development.
  • To address the need for innovative techniques to assess protein stability and mitigate risks.
  • To introduce and discuss the utility of the XL-ALSOFAST experiment for analyzing therapeutic proteins.

Main Methods:

  • Utilizing one-dimensional (1D) NMR for monitoring monoclonal antibody (mAb) structural changes and protein-excipient interactions.
  • Employing 2D NMR, such as ALSOFAST-[1H-13C]-HMQC, for detecting higher-order structural (HOS) changes in mAbs.
  • Implementing the XL-ALSOFAST-[1H-13C]-HMQC experiment for enhanced sensitivity and selectivity in high molecular weight protein analysis.

Main Results:

  • 1D NMR demonstrates potential for screening protein-excipient interactions in parenteral formulations.
  • 2D NMR techniques provide superior capability for detecting HOS changes and excipient interactions.
  • The XL-ALSOFAST experiment successfully analyzes formulations of investigational proteins with improved sensitivity and artifact suppression.

Conclusions:

  • Solution NMR spectroscopy is an emerging powerful tool for biophysical characterization of protein therapeutics.
  • Optimizing NMR parameters is critical for suppressing buffer signals and enhancing protein signals in complex formulations.
  • The XL-ALSOFAST experiment is a valuable tool for studying therapeutic proteins across various molecular sizes and buffers, supporting biologics formulation development.