Large-scale mapping of bioactive peptides in structural and sequence space

Autores
Nardo, Agustina Estefanía; Añón, María Cristina; Parisi, Gustavo Daniel
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Health-enhancing potential bioactive peptide (BP) has driven an interest in food proteins as well as in the development of predictive methods. Research in this area has been especially active to use them as components in functional foods. Apparently, BPs do not have a given biological function in the containing proteins and they do not evolve under independent evolutionary constraints. In this work we performed a large-scale mapping of BPs in sequence and structural space. Using well curated BP deposited in BIOPEP database, we searched for exact matches in non-redundant sequences databases. Proteins containing BPs, were used in fold-recognition methods to predict the corresponding folds and BPs occurrences were mapped. We found that fold distribution of BP occurrences possibly reflects sequence relative abundance in databases. However, we also found that proteins with 5 or more than 5 BP in their sequences correspond to well populated protein folds, called superfolds. Also, we found that in well populated superfamilies, BPs tend to adopt similar locations in the protein fold, suggesting the existence of hotspots. We think that our results could contribute to the development of new bioinformatics pipeline to improve BP detection.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
Materia
Ingeniería Química
Bioactive peptides
Food
Superfolds
Hot-spots
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/98334
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/98334
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Large-scale mapping of bioactive peptides in structural and sequence spaceNardo, Agustina EstefaníaAñón, María CristinaParisi, Gustavo DanielIngeniería QuímicaBioactive peptidesFoodSuperfoldsHot-spotsHealth-enhancing potential bioactive peptide (BP) has driven an interest in food proteins as well as in the development of predictive methods. Research in this area has been especially active to use them as components in functional foods. Apparently, BPs do not have a given biological function in the containing proteins and they do not evolve under independent evolutionary constraints. In this work we performed a large-scale mapping of BPs in sequence and structural space. Using well curated BP deposited in BIOPEP database, we searched for exact matches in non-redundant sequences databases. Proteins containing BPs, were used in fold-recognition methods to predict the corresponding folds and BPs occurrences were mapped. We found that fold distribution of BP occurrences possibly reflects sequence relative abundance in databases. However, we also found that proteins with 5 or more than 5 BP in their sequences correspond to well populated protein folds, called superfolds. Also, we found that in well populated superfamilies, BPs tend to adopt similar locations in the protein fold, suggesting the existence of hotspots. We think that our results could contribute to the development of new bioinformatics pipeline to improve BP detection.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2018-01-19info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1-14http://sedici.unlp.edu.ar/handle/10915/98334enginfo:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/86386info:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0191063info:eu-repo/semantics/altIdentifier/issn/1932-6203info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0191063info:eu-repo/semantics/altIdentifier/hdl/11336/86386info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-11-26T09:58:28Zoai:sedici.unlp.edu.ar:10915/98334Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-11-26 09:58:28.725SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Large-scale mapping of bioactive peptides in structural and sequence space
title Large-scale mapping of bioactive peptides in structural and sequence space
spellingShingle Large-scale mapping of bioactive peptides in structural and sequence space
Nardo, Agustina Estefanía
Ingeniería Química
Bioactive peptides
Food
Superfolds
Hot-spots
title_short Large-scale mapping of bioactive peptides in structural and sequence space
title_full Large-scale mapping of bioactive peptides in structural and sequence space
title_fullStr Large-scale mapping of bioactive peptides in structural and sequence space
title_full_unstemmed Large-scale mapping of bioactive peptides in structural and sequence space
title_sort Large-scale mapping of bioactive peptides in structural and sequence space
dc.creator.none.fl_str_mv Nardo, Agustina Estefanía
Añón, María Cristina
Parisi, Gustavo Daniel
author Nardo, Agustina Estefanía
author_facet Nardo, Agustina Estefanía
Añón, María Cristina
Parisi, Gustavo Daniel
author_role author
author2 Añón, María Cristina
Parisi, Gustavo Daniel
author2_role author
author
dc.subject.none.fl_str_mv Ingeniería Química
Bioactive peptides
Food
Superfolds
Hot-spots
topic Ingeniería Química
Bioactive peptides
Food
Superfolds
Hot-spots
dc.description.none.fl_txt_mv Health-enhancing potential bioactive peptide (BP) has driven an interest in food proteins as well as in the development of predictive methods. Research in this area has been especially active to use them as components in functional foods. Apparently, BPs do not have a given biological function in the containing proteins and they do not evolve under independent evolutionary constraints. In this work we performed a large-scale mapping of BPs in sequence and structural space. Using well curated BP deposited in BIOPEP database, we searched for exact matches in non-redundant sequences databases. Proteins containing BPs, were used in fold-recognition methods to predict the corresponding folds and BPs occurrences were mapped. We found that fold distribution of BP occurrences possibly reflects sequence relative abundance in databases. However, we also found that proteins with 5 or more than 5 BP in their sequences correspond to well populated protein folds, called superfolds. Also, we found that in well populated superfamilies, BPs tend to adopt similar locations in the protein fold, suggesting the existence of hotspots. We think that our results could contribute to the development of new bioinformatics pipeline to improve BP detection.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
description Health-enhancing potential bioactive peptide (BP) has driven an interest in food proteins as well as in the development of predictive methods. Research in this area has been especially active to use them as components in functional foods. Apparently, BPs do not have a given biological function in the containing proteins and they do not evolve under independent evolutionary constraints. In this work we performed a large-scale mapping of BPs in sequence and structural space. Using well curated BP deposited in BIOPEP database, we searched for exact matches in non-redundant sequences databases. Proteins containing BPs, were used in fold-recognition methods to predict the corresponding folds and BPs occurrences were mapped. We found that fold distribution of BP occurrences possibly reflects sequence relative abundance in databases. However, we also found that proteins with 5 or more than 5 BP in their sequences correspond to well populated protein folds, called superfolds. Also, we found that in well populated superfamilies, BPs tend to adopt similar locations in the protein fold, suggesting the existence of hotspots. We think that our results could contribute to the development of new bioinformatics pipeline to improve BP detection.
publishDate 2018
dc.date.none.fl_str_mv 2018-01-19
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/98334
url http://sedici.unlp.edu.ar/handle/10915/98334
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/86386
info:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0191063
info:eu-repo/semantics/altIdentifier/issn/1932-6203
info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0191063
info:eu-repo/semantics/altIdentifier/hdl/11336/86386
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
1-14
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.011256

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