Fluorinated Amino Acids in Peptide and Protein Assembly

Abstract

Abstract Despite its low abundance in naturally occurring biomolecules, fluorine's often favorable impact on pharmacokinetic and biological properties makes it an outstanding element. In fact, fluorination has found its way into peptide & protein science with paramount interest for biochemical and pharmaceutical applications. The introduction of fluorine can drastically conduct appropriate folding and self‐assembly as indispensable criterion for biomolecular recognition. Peptides and proteins carrying fluorine as an amino acid side chain substituent have been the focus of numerous studies in recent years with scientific breakthroughs on structural stability and preparation of novel fluorinated peptide‐based biomaterials. However, our current understanding of how side chain fluorination affects structure formation and, thus, the biological activity of peptides and proteins is confined. This book chapter provides a brief yet comprehensive introduction to this research field including state‐of‐the‐art techniques for the determination of hydrophobic properties of fluorinated amino acids used to design and fine‐tune peptide assembly and protein folding. Foundational and unique properties of these artificial biomolecules are discussed by constituting both the growing utility and necessity of fluorinated amino acids for the de novo design of peptide‐based materials and drugs.