The search for a peptide ligand targeting the lipolytic enzyme cutinase

Autores
Breccia, Javier Dario; Krook, Margareta; Ohlin, Mats; Hatti-Kaul, Rajni
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Lund University; Suecia
Fil: Krook, Margareta. Chemel AB; Suecia
Fil: Ohlin, Mats. Lund University; Suecia
Fil: Hatti-Kaul, Rajni. Lund University; Suecia
Materia
Cutinase
Cyclic Nonapeptide Library
Phage Display
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/81799
Acceder
id CONICETDig_132fb1bd5650699ce19b0bef316c6764
oai_identifier_str oai:ri.conicet.gov.ar:11336/81799
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The search for a peptide ligand targeting the lipolytic enzyme cutinaseBreccia, Javier DarioKrook, MargaretaOhlin, MatsHatti-Kaul, RajniCutinaseCyclic Nonapeptide LibraryPhage Displayhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2A 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.Fil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Lund University; SueciaFil: Krook, Margareta. Chemel AB; SueciaFil: Ohlin, Mats. Lund University; SueciaFil: Hatti-Kaul, Rajni. Lund University; SueciaElsevier Science Inc2003-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/81799Breccia, 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; 244-2490141-0229CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022903001182info:eu-repo/semantics/altIdentifier/doi/10.1016/S0141-0229(03)00118-2info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:00:06Zoai:ri.conicet.gov.ar:11336/81799instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 12:00:06.891CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The search for a peptide ligand targeting the lipolytic enzyme cutinase
title The search for a peptide ligand targeting the lipolytic enzyme cutinase
spellingShingle The search for a peptide ligand targeting the lipolytic enzyme cutinase
Breccia, Javier Dario
Cutinase
Cyclic Nonapeptide Library
Phage Display
title_short The search for a peptide ligand targeting the lipolytic enzyme cutinase
title_full The search for a peptide ligand targeting the lipolytic enzyme cutinase
title_fullStr The search for a peptide ligand targeting the lipolytic enzyme cutinase
title_full_unstemmed The search for a peptide ligand targeting the lipolytic enzyme cutinase
title_sort The search for a peptide ligand targeting the lipolytic enzyme cutinase
dc.creator.none.fl_str_mv Breccia, Javier Dario
Krook, Margareta
Ohlin, Mats
Hatti-Kaul, Rajni
author Breccia, Javier Dario
author_facet Breccia, Javier Dario
Krook, Margareta
Ohlin, Mats
Hatti-Kaul, Rajni
author_role author
author2 Krook, Margareta
Ohlin, Mats
Hatti-Kaul, Rajni
author2_role author
author
author
dc.subject.none.fl_str_mv Cutinase
Cyclic Nonapeptide Library
Phage Display
topic Cutinase
Cyclic Nonapeptide Library
Phage Display
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv 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.
Fil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Lund University; Suecia
Fil: Krook, Margareta. Chemel AB; Suecia
Fil: Ohlin, Mats. Lund University; Suecia
Fil: Hatti-Kaul, Rajni. Lund University; Suecia
description 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.
publishDate 2003
dc.date.none.fl_str_mv 2003-08
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/81799
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
0141-0229
CONICET Digital
CONICET
url http://hdl.handle.net/11336/81799
identifier_str_mv 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
0141-0229
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022903001182
info:eu-repo/semantics/altIdentifier/doi/10.1016/S0141-0229(03)00118-2
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846782325234335744
score 12.982451

Publicaciones similares