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Issue 6, 2012
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Fluorinated amino acids: compatibility with native protein structures and effects on protein–protein interactions

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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 (245 references).

Graphical abstract: Fluorinated amino acids: compatibility with native protein structures and effects on protein–protein interactions

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Article information


Submitted
06 Sep 2011
First published
30 Nov 2011

Chem. Soc. Rev., 2012,41, 2135-2171
Article type
Critical Review

Fluorinated amino acids: compatibility with native protein structures and effects on proteinprotein interactions

M. Salwiczek, E. K. Nyakatura, U. I. M. Gerling, S. Ye and B. Koksch, Chem. Soc. Rev., 2012, 41, 2135
DOI: 10.1039/C1CS15241F

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