Title of article
The search for a peptide ligand targeting the lipolytic enzyme cutinase
Author/Authors
Javier D. Breccia، نويسنده , , Margareta Krook، نويسنده , , Mats Ohlin، نويسنده , , Rajni Hatti-Kaul، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2003
Pages
6
From page
244
To page
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 the study and purification of cutinase.
Keywords
Cutinase , Cyclic nonapeptide library , phage display
Journal title
Enzyme and Microbial Technology
Serial Year
2003
Journal title
Enzyme and Microbial Technology
Record number
1173820
Link To Document