Advanced

Hydrophobic peptide tags as tools in bioseparation

Fexby, Sara LU and Bülow, Leif LU (2004) In Trends in Biotechnology 22(10). p.511-516
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Trends in Biotechnology
volume
22
issue
10
pages
511 - 516
publisher
Elsevier
external identifiers
  • pmid:15450744
  • wos:000224474100009
  • scopus:4644290642
ISSN
0167-7799
DOI
10.1016/j.tibtech.2004.08.005
language
English
LU publication?
yes
id
7f80ae48-c4cc-4768-bc9e-29e59d643838 (old id 140984)
date added to LUP
2007-07-16 09:13:06
date last changed
2017-07-30 03:37:48
@article{7f80ae48-c4cc-4768-bc9e-29e59d643838,
  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.},
  author       = {Fexby, Sara and Bülow, Leif},
  issn         = {0167-7799},
  language     = {eng},
  number       = {10},
  pages        = {511--516},
  publisher    = {Elsevier},
  series       = {Trends in Biotechnology},
  title        = {Hydrophobic peptide tags as tools in bioseparation},
  url          = {http://dx.doi.org/10.1016/j.tibtech.2004.08.005},
  volume       = {22},
  year         = {2004},
}