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The search for a peptide ligand targeting the lipolytic enzyme cutinase

Breccia, J.; Krook, M.; Ohlin, Mats LU and Hatti-Kaul, Rajni LU (2003) In Enzyme and Microbial Technology 33(2-3). p.244-249
Abstract
A constrained nonapeptide phage display library was evaluated as a potential source of affinity ligand(s) for purification of cutinase, a lipolytic enzyme. After seven cycles of biopanning, 500 clones were isolated and individually tested for their capability to interact with cutinase. Three out of six sequenced clones carrying a cutinase-specific constrained peptide showed the same insert sequence (CRLHHWRYC). Sequences of two of the other clones highlighted a LXXW motif as a critical determinant in the make-up of a cutinase-specific sequence. Although the affinity of the most commonly found peptide for cutinase is low, we suggest that LXXW motif may be a suitable starting point in the development of affinity peptides suitable for use in... (More)
A constrained nonapeptide phage display library was evaluated as a potential source of affinity ligand(s) for purification of cutinase, a lipolytic enzyme. After seven cycles of biopanning, 500 clones were isolated and individually tested for their capability to interact with cutinase. Three out of six sequenced clones carrying a cutinase-specific constrained peptide showed the same insert sequence (CRLHHWRYC). Sequences of two of the other clones highlighted a LXXW motif as a critical determinant in the make-up of a cutinase-specific sequence. Although the affinity of the most commonly found peptide for cutinase is low, we suggest that LXXW motif may be a suitable starting point in the development of affinity peptides suitable for use in the study and purification of cutinase. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Enzyme and Microbial Technology
volume
33
issue
2-3
pages
244 - 249
publisher
Elsevier
external identifiers
  • wos:000184588900015
  • scopus:0142043929
ISSN
0141-0229
DOI
10.1016/S0141-0229(03)00118-2
language
English
LU publication?
yes
id
c015698f-e696-4bf6-aac8-f9ee30635e5f (old id 129114)
date added to LUP
2007-06-27 11:27:23
date last changed
2017-01-01 04:49:06
@article{c015698f-e696-4bf6-aac8-f9ee30635e5f,
  abstract     = {A constrained nonapeptide phage display library was evaluated as a potential source of affinity ligand(s) for purification of cutinase, a lipolytic enzyme. After seven cycles of biopanning, 500 clones were isolated and individually tested for their capability to interact with cutinase. Three out of six sequenced clones carrying a cutinase-specific constrained peptide showed the same insert sequence (CRLHHWRYC). Sequences of two of the other clones highlighted a LXXW motif as a critical determinant in the make-up of a cutinase-specific sequence. Although the affinity of the most commonly found peptide for cutinase is low, we suggest that LXXW motif may be a suitable starting point in the development of affinity peptides suitable for use in the study and purification of cutinase.},
  author       = {Breccia, J. and Krook, M. and Ohlin, Mats and Hatti-Kaul, Rajni},
  issn         = {0141-0229},
  language     = {eng},
  number       = {2-3},
  pages        = {244--249},
  publisher    = {Elsevier},
  series       = {Enzyme and Microbial Technology},
  title        = {The search for a peptide ligand targeting the lipolytic enzyme cutinase},
  url          = {http://dx.doi.org/10.1016/S0141-0229(03)00118-2},
  volume       = {33},
  year         = {2003},
}