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Trends Biotechnol. 2004 Oct;22(10):511-6.

Hydrophobic peptide tags as tools in bioseparation.

Author information

1
Laboratoire de Technologie Enzymatique, UMR 6022 du CNRS, Université de Technologie de Compiègne, B.P. 20529, F-60205 Compiègne Cedex, France. sarafexby@yahoo.se

Abstract

Hydrophobic interactions are highly selective, and differences in surface hydrophobicities between proteins can be used as an efficient handle to facilitate protein isolation. Aromatic amino acid residues are of particular importance for molecular recognition because they have a key role in several biological functions. The hydrophobicity of a protein can easily be altered with minor genetic modifications, such as site-directed mutagenesis or fusions of hydrophobic peptide tags. An important advantage of hydrophobic peptide tags over traditional affinity tags is the possibility of exploring simple and inexpensive bioseparation materials. Recent results demonstrate the potential of hydrophobic interaction chromatography and aqueous two-phase systems as tools to study relative hydrophobicities of recombinant proteins with only minor alterations. This review focuses on hydrophobic peptide tags as fusion partners, which can be used as important tools in bioseparation.

PMID:
15450744
DOI:
10.1016/j.tibtech.2004.08.005
[Indexed for MEDLINE]

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