aSynPEP-DB
Parkinson's disease (PD) is the second most prevalent neurodegenerative disorder, yet effective treatments able to stop or delay disease progression remain elusive. The aggregation of a presynaptic protein, α-synuclein (aSyn), is the primary neurological hallmark of PD and, thus, a promising ta...
| Autores: | , , , , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2023 |
| País: | España |
| Institución: | Universitat Autònoma de Barcelona |
| Repositorio: | Dipòsit Digital de Documents de la UAB |
| Idioma: | inglés |
| OAI Identifier: | oai:ddd.uab.cat:304952 |
| Acceso en línea: | https://ddd.uab.cat/record/304952 https://dx.doi.org/urn:doi:10.1093/database/baad084 |
| Access Level: | acceso abierto |
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aSynPEP-DBa database of biogenic peptides for inhibiting α-synuclein aggregationPintado-Grima, Carlos|||0000-0002-8544-959XBárcenas, Oriol|||0000-0002-8439-4005Iglesias, Valentin|||0000-0002-6133-0869Santos Suárez, Jaime|||0000-0001-9045-7765Manglano-Artuñedo, ZoePallarès i Goitiz, Irantzu|||0000-0002-8205-2060Burdukiewicz, Michał|||0000-0001-8926-582XVentura, Salvador|||0000-0002-9652-6351Parkinson's disease (PD) is the second most prevalent neurodegenerative disorder, yet effective treatments able to stop or delay disease progression remain elusive. The aggregation of a presynaptic protein, α-synuclein (aSyn), is the primary neurological hallmark of PD and, thus, a promising target for therapeutic intervention. However, the lack of consensus on the molecular properties required to specifically bind the toxic species formed during aSyn aggregation has hindered the development of therapeutic molecules. Recently, we defined and experimentally validated a peptide architecture that demonstrated high affinity and selectivity in binding to aSyn toxic oligomers and fibrils, effectively preventing aSyn pathogenic aggregation. Human peptides with such properties may have neuroprotective activities and hold a huge therapeutic interest. Driven by this idea, here, we developed a discriminative algorithm for the screening of human endogenous neuropeptides, antimicrobial peptides and diet-derived bioactive peptides with the potential to inhibit aSyn aggregation. We identified over 100 unique biogenic peptide candidates and ensembled a comprehensive database (aSynPEP-DB) that collects their physicochemical features, source datasets and additional therapeutic-relevant information, including their sites of expression and associated pathways. Besides, we provide access to the discriminative algorithm to extend its application to the screening of artificial peptides or new peptide datasets. aSynPEP-DB is a unique repository of peptides with the potential to modulate aSyn aggregation, serving as a platform for the identification of previously unexplored therapeutic agents. Database URL:. 22023-01-0120232023-01-01Articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/304952https://dx.doi.org/urn:doi:10.1093/database/baad084reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengAgència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2023FI300018European Commission https://doi.org/10.13039/501100000780 952334Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 PID2019-105017RB-I00open accesshttp://purl.org/coar/access_right/c_abf2Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:3049522026-06-06T12:50:31Z |
| dc.title.none.fl_str_mv |
aSynPEP-DB a database of biogenic peptides for inhibiting α-synuclein aggregation |
| title |
aSynPEP-DB |
| spellingShingle |
aSynPEP-DB Pintado-Grima, Carlos|||0000-0002-8544-959X |
| title_short |
aSynPEP-DB |
| title_full |
aSynPEP-DB |
| title_fullStr |
aSynPEP-DB |
| title_full_unstemmed |
aSynPEP-DB |
| title_sort |
aSynPEP-DB |
| dc.creator.none.fl_str_mv |
Pintado-Grima, Carlos|||0000-0002-8544-959X Bárcenas, Oriol|||0000-0002-8439-4005 Iglesias, Valentin|||0000-0002-6133-0869 Santos Suárez, Jaime|||0000-0001-9045-7765 Manglano-Artuñedo, Zoe Pallarès i Goitiz, Irantzu|||0000-0002-8205-2060 Burdukiewicz, Michał|||0000-0001-8926-582X Ventura, Salvador|||0000-0002-9652-6351 |
| author |
Pintado-Grima, Carlos|||0000-0002-8544-959X |
| author_facet |
Pintado-Grima, Carlos|||0000-0002-8544-959X Bárcenas, Oriol|||0000-0002-8439-4005 Iglesias, Valentin|||0000-0002-6133-0869 Santos Suárez, Jaime|||0000-0001-9045-7765 Manglano-Artuñedo, Zoe Pallarès i Goitiz, Irantzu|||0000-0002-8205-2060 Burdukiewicz, Michał|||0000-0001-8926-582X Ventura, Salvador|||0000-0002-9652-6351 |
| author_role |
author |
| author2 |
Bárcenas, Oriol|||0000-0002-8439-4005 Iglesias, Valentin|||0000-0002-6133-0869 Santos Suárez, Jaime|||0000-0001-9045-7765 Manglano-Artuñedo, Zoe Pallarès i Goitiz, Irantzu|||0000-0002-8205-2060 Burdukiewicz, Michał|||0000-0001-8926-582X Ventura, Salvador|||0000-0002-9652-6351 |
| author2_role |
author author author author author author author |
| description |
Parkinson's disease (PD) is the second most prevalent neurodegenerative disorder, yet effective treatments able to stop or delay disease progression remain elusive. The aggregation of a presynaptic protein, α-synuclein (aSyn), is the primary neurological hallmark of PD and, thus, a promising target for therapeutic intervention. However, the lack of consensus on the molecular properties required to specifically bind the toxic species formed during aSyn aggregation has hindered the development of therapeutic molecules. Recently, we defined and experimentally validated a peptide architecture that demonstrated high affinity and selectivity in binding to aSyn toxic oligomers and fibrils, effectively preventing aSyn pathogenic aggregation. Human peptides with such properties may have neuroprotective activities and hold a huge therapeutic interest. Driven by this idea, here, we developed a discriminative algorithm for the screening of human endogenous neuropeptides, antimicrobial peptides and diet-derived bioactive peptides with the potential to inhibit aSyn aggregation. We identified over 100 unique biogenic peptide candidates and ensembled a comprehensive database (aSynPEP-DB) that collects their physicochemical features, source datasets and additional therapeutic-relevant information, including their sites of expression and associated pathways. Besides, we provide access to the discriminative algorithm to extend its application to the screening of artificial peptides or new peptide datasets. aSynPEP-DB is a unique repository of peptides with the potential to modulate aSyn aggregation, serving as a platform for the identification of previously unexplored therapeutic agents. Database URL:. |
| publishDate |
2023 |
| dc.date.none.fl_str_mv |
2 2023-01-01 2023 2023-01-01 |
| dc.type.none.fl_str_mv |
Article http://purl.org/coar/resource_type/c_6501 VoR http://purl.org/coar/version/c_970fb48d4fbd8a85 |
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info:eu-repo/semantics/article |
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article |
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https://ddd.uab.cat/record/304952 https://dx.doi.org/urn:doi:10.1093/database/baad084 |
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https://ddd.uab.cat/record/304952 https://dx.doi.org/urn:doi:10.1093/database/baad084 |
| dc.language.none.fl_str_mv |
Inglés eng |
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Inglés |
| language |
eng |
| dc.relation.none.fl_str_mv |
Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2023FI300018 European Commission https://doi.org/10.13039/501100000780 952334 Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 PID2019-105017RB-I00 |
| dc.rights.none.fl_str_mv |
open access http://purl.org/coar/access_right/c_abf2 https://creativecommons.org/licenses/by/4.0/ |
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info:eu-repo/semantics/openAccess |
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open access http://purl.org/coar/access_right/c_abf2 https://creativecommons.org/licenses/by/4.0/ |
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openAccess |
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application/pdf |
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reponame:Dipòsit Digital de Documents de la UAB instname:Universitat Autònoma de Barcelona |
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Universitat Autònoma de Barcelona |
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