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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
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How Sugars Protect Dry Protein Structure.

Julia A Brom1, Ruta G Petrikis1, Gary J Pielak1,2,3,4

  • 1Department of Chemistry, University of North Carolina at Chapel Hill (UNC-CH), Chapel Hill, North Carolina 27599-3290, United States.

Biochemistry
|February 21, 2023
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Summary
This summary is machine-generated.

Sugars protect proteins during drying by strengthening internal bonds and replacing water. Trehalose is ideal due to its stability, aiding in preserving protein drugs and enzymes.

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Area of Science:

  • Biochemistry
  • Protein Stabilization
  • Biophysics

Background:

  • Sugars, particularly trehalose, are used by extremotolerant organisms and industry to protect proteins from desiccation.
  • The precise mechanisms by which sugars, especially stable trehalose, protect proteins are not fully understood.
  • This knowledge gap impedes the development of new excipients and formulations for protein-based therapeutics and industrial enzymes.

Purpose of the Study:

  • To elucidate the protective mechanisms of trehalose and other sugars on protein structure during drying.
  • To investigate the role of vitrification and water retention in sugar-mediated protein protection.
  • To identify key factors contributing to trehalose's efficacy as a protein protectant.

Main Methods:

  • Liquid-observed vapor exchange nuclear magnetic resonance (LOVE NMR) to monitor protein structure.
  • Differential scanning calorimetry (DSC) to assess thermal properties.
  • Thermal gravimetric analysis (TGA) to evaluate water content and thermal stability.

Main Results:

  • Intramolecular hydrogen bonds within proteins are significantly protected by sugars.
  • Vitrification, indicated by LOVE NMR and DSC, appears to play a protective role.
  • Water retention was found to be unimportant for sugar-mediated protein protection, as shown by LOVE NMR and TGA.
  • Sugars protect protein structure during drying by enhancing intraprotein hydrogen bonds and through water replacement.

Conclusions:

  • Sugars protect protein structure during desiccation by strengthening internal hydrogen bonds and acting as water replacements.
  • Trehalose's superior protective capabilities are attributed to its inherent covalent stability.
  • Understanding these mechanisms can guide the rational design of novel formulations for stabilizing protein drugs and enzymes.