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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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Photodegradation Pathways of Protein Disulfides: Human Growth Hormone.

Daniel Steinmann1,2, Olivier Mozziconacci1,3, Rupesh Bommana1

  • 1Department of Pharmaceutical Chemistry, University of Kansas, 2095 Constant Ave,, Lawrence, Kansas, 66047, USA.

Pharmaceutical Research
|September 20, 2017
PubMed
Summary

Photodegradation of human growth hormone (hGH) revealed 60 products from disulfide bond damage, including novel cross-links. This provides crucial data for analyzing protein stability under light exposure.

Keywords:
cross-linkdisulfidehGHhuman growth hormoneoxidationpeptide cleavagephoto-degradationsomatotropinthiyl radical

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Area of Science:

  • Biochemistry
  • Photochemistry
  • Analytical Chemistry

Background:

  • Protein disulfide bonds are crucial for structure and function.
  • Understanding photodegradation is vital for protein stability analysis.
  • Human growth hormone (hGH) serves as a model protein.

Purpose of the Study:

  • To comprehensively characterize photodegradation products of protein disulfides using hGH.
  • To build a product database for general protein stability analysis.
  • To investigate light-induced disulfide degradation pathways.

Main Methods:

  • Photo-irradiation of hGH at specific wavelengths (254 nm and >295 nm).
  • Tryptic digestion of irradiated hGH.
  • Analysis of digests using High-Performance Liquid Chromatography-Mass Spectrometry (HPLC-MS) with MS2 and MS3.
  • Utilized a 75 cm nano-column for isomer resolution.

Main Results:

  • Identified and characterized 60 photodegradation products.
  • Main products include reduced Cys residues, dithiohemiacetal, thioether, and disulfide scrambling products.
  • Detected various Cys degradation products (e.g., dehydroalanine) and novel cross-links (e.g., Cys-Tyr, Cys-Ser).
  • Observed specific photo-induced fragmentation near disulfide bonds (T6-T16).

Conclusions:

  • Photodegradation of protein disulfides yields diverse products, including novel cross-links.
  • The study elucidates mechanisms of photo-product formation.
  • The generated product database aids in assessing protein stability.