- 198 pages
- English
- PDF
- Available on iOS & Android
About this book
There is a constant need for developing improved methods for introducing artificial functionalities into peptides and proteins, as the modification of peptides and proteins is one of the major routes to investigate biological function in vitro and in vivo, e.g. by introduction of spin labels or fluorophores. To improve the synthetic accessibility of chemically modified peptides and proteins a new cysteine-free Native Chemical Ligation strategy based on a photocleavable auxiliary was developed and successfully implemented. In addition, a novel protocol for labeling peptides and proteins by introducing artificial, histidine-mimicking amino acids was devised. These triazole-based building blocks were utilized for the introduction of additional metal binding sites into peptides as well as for the development of peptidic zinc sensors based on zinc finger peptide Zif268.
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Table of contents
- TABLE OF CONTENTS
- 1. INTRODUCTION
- 2. HISTIDINE-BASED ARTIFICIAL AMINO ACIDS FOR THE MODIFICATION OF METAL BINDING SITES IN BIOMOLECULES
- 3. DIFLUORINATED FATTY ACIDS
- 4. DEVELOPMENT OF A NEW AUXILIARY-MEDIATED LIGATION STRATEGY
- 5. SUMMARY
- 6. EXPERIMENTAL PART
- ABBREVIATIONS
- REFERENCES
- ACKNOWLEDGEMENT
- CURRICULUM VITAE