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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/129114
- author
- Breccia, J.
; Krook, M.
; Ohlin, Mats
LU
and Hatti-Kaul, Rajni
LU
- organization
- publishing date
- 2003
- 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
- 2016-04-01 12:04:53
- date last changed
- 2022-01-26 22:29:42
@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}},
doi = {{10.1016/S0141-0229(03)00118-2}},
volume = {{33}},
year = {{2003}},
}