Fluorinated amino acids: Compatibility with native protein structures and effects on protein-protein interactions

Mario Salwiczek, Elisabeth K. Nyakatura, Ulla I.M. Gerling, Shijie Ye, Beate Koksch

Research output: Contribution to journalReview article

234 Scopus citations

Abstract

Fluorinated analogues of the canonical α-L-amino acids have gained widespread attention as building blocks that may endow peptides and proteins with advantageous biophysical, chemical and biological properties. This critical review covers the literature dealing with investigations of peptides and proteins containing fluorinated analogues of the canonical amino acids published over the course of the past decade including the late nineties. It focuses on side-chain fluorinated amino acids, the carbon backbone of which is identical to their natural analogues. Each class of amino acids - aliphatic, aromatic, charged and polar as well as proline - is presented in a separate section. General effects of fluorine on essential properties such as hydrophobicity, acidity/basicity and conformation of the specific side chains and the impact of these altered properties on stability, folding kinetics and activity of peptides and proteins are discussed.

Original languageEnglish (US)
Pages (from-to)2135-2171
Number of pages37
JournalChemical Society Reviews
Volume41
Issue number6
DOIs
StatePublished - Mar 21 2012
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)

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