dd67907e9dac39c46bde50864c77954c pmc_10059018.pdf d524015ec87b8f9a9b8c1fa425c21248227eb48c pmc_10059018.pdf f6de16d7afe3bae03f1c84650d305733310f9d886893082199dc351981035623 pmc_10059018.pdf Title: Development of Small Molecules Targeting -Synuclein Aggregation: A Promising Strategy to Treat Parkinson’s Disease Subject: Parkinson’s disease, the second most common neurodegenerative disorder worldwide, is characterized by the accumulation of protein deposits in the dopaminergic neurons. These deposits are primarily composed of aggregated forms of -Synuclein (-Syn). Despite the extensive research on this disease, only symptomatic treatments are currently available. However, in recent years, several compounds, mainly of an aromatic character, targeting -Syn self-assembly and amyloid formation have been identified. These compounds, discovered by different approaches, are chemically diverse and exhibit a plethora of mechanisms of action. This work aims to provide a historical overview of the physiopathology and molecular aspects associated with Parkinson’s disease and the current trends in small compound development to target -Syn aggregation. Although these molecules are still under development, they constitute an important step toward discovering effective anti-aggregational therapies for Parkinson’s disease. Keywords: Parkinson’s disease; aggregation; -Synuclein; amyloid; inhibitor Author: Samuel Peña-Díaz, Javier García-Pardo and Salvador Ventura Creator: LaTeX with hyperref Producer: pdfTeX-1.40.21 CreationDate: Fri Mar 3 18:44:15 2023 CET ModDate: Fri Mar 3 18:54:25 2023 CET Tagged: no UserProperties: no Suspects: no Form: none JavaScript: no Pages: 34 Encrypted: no Page size: 595.276 x 841.89 pts (A4) Page rot: 0 File size: 4219443 bytes Optimized: no PDF version: 1.7 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- CZOINJ+EURB10 Type 1 Builtin yes yes no 10 0 WLENKM+VnURWPalladioL-Bold Type 1 Custom yes yes no 14 0 LWJOET+VnURWPalladioL Type 1 Custom yes yes no 19 0 GOCQIR+EURM10 Type 1 Builtin yes yes no 23 0 IRMTWA+URWPalladioL-Bold Type 1 Custom yes yes no 27 0 WCCNPO+URWPalladioL-Roma Type 1 Custom yes yes no 32 0 GYRYYN+URWPalladioL-Ital Type 1 Custom yes yes no 36 0 IHGURL+EURM7 Type 1 Builtin yes yes no 40 0 IAFAOG+TimesNewRomanPS-BoldItalicMT Type 1C WinAnsi yes yes no 59 0 OALKMI+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 93 0 OALKNJ+PalatinoLinotype CID TrueType Identity-H yes yes yes 96 0 OALKNK+PalatinoLinotype TrueType WinAnsi yes yes no 102 0 OALKNM+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 105 0 OALKMI+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 116 0 OALKNJ+PalatinoLinotype CID TrueType Identity-H yes yes yes 119 0 OALKNK+PalatinoLinotype TrueType WinAnsi yes yes no 125 0 OALKNM+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 128 0 OALKMI+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 144 0 OALKNJ+PalatinoLinotype CID TrueType Identity-H yes yes yes 147 0 OALKNK+PalatinoLinotype TrueType WinAnsi yes yes no 153 0 OALKNM+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 156 0 OALKMI+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 166 0 OALKNJ+PalatinoLinotype CID TrueType Identity-H yes yes yes 169 0 OALKNK+PalatinoLinotype TrueType WinAnsi yes yes no 175 0 OALKNM+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 178 0 OALKMI+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 191 0 OALKNJ+PalatinoLinotype CID TrueType Identity-H yes yes yes 194 0 OALKNK+PalatinoLinotype TrueType WinAnsi yes yes no 200 0 OALKNM+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 203 0 OALKMI+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 218 0 OALKNJ+PalatinoLinotype CID TrueType Identity-H yes yes yes 221 0 OALKNK+PalatinoLinotype TrueType WinAnsi yes yes no 227 0 OALKNM+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 230 0 OALKMI+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 241 0 OALKNJ+PalatinoLinotype CID TrueType Identity-H yes yes yes 244 0 OALKNK+PalatinoLinotype TrueType WinAnsi yes yes no 250 0 OALKNM+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 253 0 VPWCDI+VnURWPalladioL-Italic Type 1 Custom yes yes no 282 0 Jhove (Rel. 1.28.0, 2023-05-18) Date: 2024-02-02 02:35:55 CET RepresentationInformation: pmc_10059018.pdf ReportingModule: PDF-hul, Rel. 1.12.4 (2023-03-16) LastModified: 2023-09-22 02:16:41 CEST Size: 4219443 Format: PDF Version: 1.7 Status: Well-Formed and valid SignatureMatches: PDF-hul MIMEtype: application/pdf PDFMetadata: Objects: 1229 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: PageLayout: SinglePage PageMode: UseNone Outlines: Item: Title: Introduction Destination: section.1 Item: Title: Historical Overview Destination: section.2 Item: Title: Symptomatology Destination: section.3 Item: Title: Risk Factors and Genetics of Parkinson’s Disease Destination: section.4 Item: Title: Molecular Mechanism Implicated in PD Development Destination: section.5 Item: Title: Alpha-Synuclein Destination: section.6 Item: Title: New Therapies: Modulating -Synuclein Aggregation Destination: section.7 Children: Item: Title: Polyphenolic Scaffolds Destination: subsection.7.1 Item: Title: Repositioned Compounds Destination: subsection.7.2 Item: Title: Compounds Developed by Rational Design Destination: subsection.7.3 Item: Title: Compounds Derived from High-Throughput Screenings Destination: subsection.7.4 Item: Title: Structure-Based Strategies for Drug Discovery Destination: subsection.7.5 Item: Title: Conclusions Destination: section.8 Item: Title: References Destination: section.8 Info: Title: Development of Small Molecules Targeting -Synuclein Aggregation: A Promising Strategy to Treat Parkinson’s Disease Author: Samuel Peña-Díaz, Javier García-Pardo and Salvador Ventura Subject: Parkinson’s disease, the second most common neurodegenerative disorder worldwide, is characterized by the accumulation of protein deposits in the dopaminergic neurons. These deposits are primarily composed of aggregated forms of -Synuclein (-Syn). Despite the extensive research on this disease, only symptomatic treatments are currently available. However, in recent years, several compounds, mainly of an aromatic character, targeting -Syn self-assembly and amyloid formation have been identified. These compounds, discovered by different approaches, are chemically diverse and exhibit a plethora of mechanisms of action. This work aims to provide a historical overview of the physiopathology and molecular aspects associated with Parkinson’s disease and the current trends in small compound development to target -Syn aggregation. Although these molecules are still under development, they constitute an important step toward discovering effective anti-aggregational therapies for Parkinson’s disease. 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