Physical Methods to Characterize Pharmaceutical Proteins

1. Front Matter

   Pages i-xvii

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2. Application of Fluorescence Spectroscopy for Determining the Structure and Function of Proteins

   • Wim Jiskoot, Vladimir Hlady, John J. Naleway, James N. Herron

   Pages 1-63

3. Structural Information on Proteins from Circular Dichroism Spectroscopy Possibilities and Limitations

   • Michael Bloemendal, W. Curtis Johnson Jr.

   Pages 65-100

4. Fourier Transform Infrared Spectroscopy Investigations of Protein Structure

   • E. A. Cooper, K. Knutson

   Pages 101-143

5. Mass Spectrometry in Protein Structural Analysis

   • Peter Roepstorff

   Pages 145-177

6. Two-, Three-, and Four-Dimensional Nuclear Magnetic Resonance Spectroscopy of Protein Pharmaceuticals

   • David G. Vander Velde, James Matsuura, Mark C. Manning

   Pages 179-218

7. Thermodynamic Strategies for Rational Protein and Drug Design

   • Kenneth P. Murphy, Ernesto Freire

   Pages 219-241

8. Chromatographic Techniques for the Characterization of Proteins

   • Joost J. M. Holthuis, Reinoud J. Driebergen

   Pages 243-299

9. Capillary Electrophoresis of Proteins

   • Tom A. A. M. van de Goor

   Pages 301-327

10. Applying Genetic Engineering to the Structural Analysis of Proteins

    • Paul T. Hamilton

    Pages 329-350

11. Back Matter

    Pages 351-362

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Proteins are still gaining importance in the pharmaceutical world, where they are used to improve our arsenal of therapeutic drugs and vaccines and as diagnostic tools. Proteins are different from "traditional" low-molecular-weight drugs. As a group, they exhibit a number of biopharmaceutical and formulation problems. These problems have drawn considerable interest from both industrial and aca­ demic environments, forcing pharmaceutical scientists to explore a domain previ­ ously examined only by peptide and protein chemists. Biopharmaceutical aspects of proteins, e.g., low oral bioavailability, have been extensively investigated. Although all possible conventional routes of ad­ ministration have been examined for proteins, no real, generally applicable alter­ native to parenteral administration in order to achieve systemic effects has yet been discovered. Several of these biopharmaceutical options have been discussed in Volume 4 of this series, Biological Barriers to Protein Delivery. Proteins are composed of many amino acids, several of which are notorious for their chemical instability. Rational design of formulations that optimize the native structure and/or bioactivity of a protein is therefore of great importance when long shelf life is required, as it is for pharmaceutical products. This issue has also been examined in two prior volumes of this series: Volume 2: Stability of Protein Pharmaceuticals (Part A) and Volume 5: Stability and Characterization of Protein and Peptide Drugs.

• fluorescence
• infrared spectroscopy
• magnetic resonance
• proteins
• spectroscopy

• University of Utah, Salt Lake City, USA

  James N. Herron

• National Institute of Public Health and Environmental Protection, Bilthoven, The Netherlands

  Wim Jiskoot

• Groningen-Utrecht Institute for Drug Exploration, Utrecht University, and Utrecht Institute for Pharmaceutical Sciences, Utrecht, The Netherlands

  Daan J. A. Crommelin

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