Artículo
The search for a peptide ligand targeting the lipolytic enzyme cutinase
Fecha de publicación:
08/2003
Editorial:
Elsevier Science Inc
Revista:
Enzyme and Microbial Technology
ISSN:
0141-0229
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
Palabras clave:
Cutinase
,
Cyclic Nonapeptide Library
,
Phage Display
Archivos asociados
Licencia
Identificadores
Colecciones
Articulos(INCITAP)
Articulos de INST.D/CS D/L/TIERRA Y AMBIENTALES D/L/PAMPA
Articulos de INST.D/CS D/L/TIERRA Y AMBIENTALES D/L/PAMPA
Citación
Breccia, Javier Dario; Krook, Margareta; Ohlin, Mats; Hatti-Kaul, Rajni; The search for a peptide ligand targeting the lipolytic enzyme cutinase; Elsevier Science Inc; Enzyme and Microbial Technology; 33; 2-3; 8-2003; 244-249
Compartir
Altmétricas