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Related Concept Videos

2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

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Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other...
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2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

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Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
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2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

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Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
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Raman Spectroscopy: Overview01:20

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The underlying principle of Raman spectroscopy is based on the interaction between light and matter, specifically molecules' inelastic scattering of photons. When a monochromatic beam of light, typically from a laser source, interacts with a sample, most scattered light has the same frequency as the incident light. This is known as Rayleigh scattering.
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Raman Spectroscopy Instrumentation: Overview01:26

Raman Spectroscopy Instrumentation: Overview

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A conventional Raman spectrophotometer includes a laser source, a sample holding system, a wavelength selector, and a detector.
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Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...
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Raman Spectroscopy with 2D Perturbation Correlation Moving Windows for the Characterization of Heparin-Amyloid

David J Townsend1, David A Middleton1, Lorna Ashton1

  • 1Department of Chemistry, Lancaster University, Lancaster LA1 4YB, United Kingdom.

Analytical Chemistry
|September 16, 2020
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Summary

Glycosaminoglycan (GAG)-protein interactions influence amyloid fibril clearance. This study uses Raman spectroscopy to reveal how heparin affects apolipoprotein A-I (apoA-I) structure during amyloid formation, offering insights into atherosclerosis.

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Area of Science:

  • Biochemistry
  • Spectroscopy
  • Biophysics

Background:

  • Glycosaminoglycan (GAG)-protein interactions significantly impact amyloid fibril formation and clearance in various amyloidosis conditions.
  • Understanding the molecular mechanisms of these interactions is crucial for developing therapeutic strategies against amyloid diseases.
  • Current analytical methods often lack the capability to simultaneously track protein conformational changes and characterize GAG binding.

Purpose of the Study:

  • To investigate the role of heparin in the fibril formation of apolipoprotein A-I (apoA-I), a protein implicated in atherosclerosis.
  • To develop and apply an analytical approach capable of identifying protein structural transitions concurrently with heparin interactions.
  • To elucidate the molecular details of GAG-protein interactions in the context of amyloidogenesis.

Main Methods:

  • Utilized Raman spectroscopy, a vibrational spectroscopy technique, to monitor molecular changes.
  • Applied two-dimensional (2D) perturbation correlation moving window (2DPCMW) analysis to interpret spectroscopic data.
  • Investigated the fibril formation of apoA-I under varying pH and heparin concentrations.

Main Results:

  • Successfully identified alterations in the secondary structure of apoA-I during pH- and heparin-induced fibril formation.
  • Observed distinct changes in specific heparan sulfate moieties through Raman peak shifts and intensity variations.
  • Demonstrated that the nature of protein-heparin interactions is dependent on heparin concentration.

Conclusions:

  • Raman spectroscopy combined with 2DPCMW analysis provides valuable mechanistic insights into GAG-mediated amyloid fibril formation.
  • Heparin concentration plays a critical role in modulating apoA-I structural changes and fibril formation.
  • This approach offers a powerful tool for studying GAG-protein interactions in amyloid diseases.