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Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
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Published on: April 14, 2015

Solid state fluorescence of lyophilized proteins.

Ranjini Ramachander1, Yijia Jiang, Cynthia Li

  • 1Product and Process Development, One Amgen Center Drive, Thousand Oaks, CA 91320, USA. ranjinir@amgen.com

Analytical Biochemistry
|March 11, 2008
PubMed
Summary
This summary is machine-generated.

Solid-state fluorescence spectroscopy using the Cary-Eclipse system can monitor structural changes in lyophilized proteins. This technique shows promise for assessing protein stability and aiding formulation development.

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Area of Science:

  • Biophysical Chemistry
  • Protein Science
  • Analytical Chemistry

Background:

  • Fluorescence spectroscopy is sensitive to protein tertiary structure and tryptophan environment, aiding solution-state conformation and stability studies.
  • Analyzing lyophilized proteins via fluorescence is challenging due to light scattering and technical hurdles.

Purpose of the Study:

  • To investigate the feasibility of analyzing lyophilized proteins using solid-state fluorescence spectroscopy.
  • To monitor heat-induced degradation in lyophilized protein therapeutics and correlate findings with solution-state behavior.

Main Methods:

  • Utilized the Cary-Eclipse spectrofluorometer to measure intrinsic fluorescence of lyophilized protein therapeutics.
  • Subjected lyophilized protein samples to accelerated degradation via heat treatment.
  • Performed fluorescence spectroscopy, circular dichroism, and size exclusion chromatography on both solid-state and reconstituted samples.

Main Results:

  • Obtained reproducible fluorescence spectra from lyophilized proteins under accelerated degradation conditions.
  • Correlated solid-state fluorescence changes with solution-state tertiary structural alterations and reconstituted protein properties.
  • Observed a correlation between decreased fluorescence intensity and increased protein aggregation (tetramer formation) in solution, indicating reduced stability.

Conclusions:

  • Solid-state intrinsic protein fluorescence measurements are feasible using the Cary-Eclipse system with a specialized holder.
  • This method shows potential for long-term stability studies and formulation development of lyophilized protein therapeutics.
  • The technique offers a valuable approach to assess protein structural integrity in the solid state.