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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 discr Keywords: Author: Carlos Pintado-Grima,Oriol B"00E1rcenas,Valentín Iglesias,Jaime Santos,Zoe Manglano-Artuñedo,Irantzu Pallarès,Michał Burdukiewicz, Salvador Ventura Creator: LuaLaTeX with hyperref package Producer: LuaLaTeX CreationDate: Thu Nov 23 07:51:54 2023 CET ModDate: Mon Nov 27 10:47:51 2023 CET Custom Metadata: yes Metadata Stream: yes Tagged: yes UserProperties: no Suspects: no Form: AcroForm JavaScript: no Pages: 9 Encrypted: no Page size: 595.276 x 782.362 pts Page rot: 0 File size: 2585830 bytes Optimized: yes PDF version: 1.6 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- GHAXJD+UniversLTStd-Bold CID Type 0C Identity-H yes yes yes 1741 0 XVZVYO+LMRoman10-Regular CID Type 0C Identity-H yes yes yes 1744 0 QWULHZ+LatinModernMath-Regular CID Type 0C Identity-H yes yes yes 1747 0 TMABBV+UniversLTStd-Cn CID Type 0C Identity-H yes yes yes 1750 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Published by Oxford University Press. OUP Publishing 2023-11-23T12:21:54+05:30 en-US DOI: https://doi.org/10.1093/database/baad084, Database, 00, 00, Published xx xxx xxx. Abstract: 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 discr aSynPEP-DB: a database of biogenic peptides for inhibiting $\upalpha $-synuclein aggregation Carlos Pintado-Grima,Oriol B"00E1rcenas,Valentín Iglesias,Jaime Santos,Zoe Manglano-Artuñedo,Irantzu Pallarès,Michał Burdukiewicz, Salvador Ventura 2023-11-23T12:21:54+05:30 LuaLaTeX with hyperref package 2023-11-27T15:17:51+05:30 2023-11-27T15:17:51+05:30 uuid:bb13eaea-3ef2-4059-859b-18200a3ea882 uuid:d19af0c0-0501-411f-ac70-3372e22f1de7 default 1 converted uuid:462b626c-9059-4005-9054-6c905f205418 converted to PDF/A-3a Preflight 2023-11-27T15:17:13+05:30 converted uuid:ce0b6545-7ef0-4865-8715-017fb46dd161 converted to PDF/A-3a Preflight 2023-11-27T15:17:51+05:30 three Journal 00 00 1758-0463 https://doi.org/10.1093/database/baad084 https://doi.org/https://doi.org/10.1093/database/baad084 9 9 3 A Adobe PDF Schema pdf http://ns.adobe.com/pdf/1.3/ Trapped Text internal A name object indicating whether the document has been modified to include trapping information XMP Media Management Schema xmpMM http://ns.adobe.com/xap/1.0/mm/ DocumentID URI internal UUID based identifier for all versions and renditions of a document InstanceID URI internal UUID based identifier for specific incarnation of a document VersionID Text internal Document version identifier RenditionClass RenditionClass internal The manner in which a document is rendered internal The common identifier for all versions and renditions of a document. 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