Alpha-Synuclein—Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity
Alpha-synuclein (αS) is an extensively studied protein due to its involvement in a group of neurodegenerative disorders, including Parkinson′s disease, and its documented ability to undergo aberrant self-aggregation resulting in the formation of amyloid-like fibrils. In dilute solution, the protein...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-11-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/25/23/5625 |
| _version_ | 1797546272111984640 |
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| author | Mariapina D’Onofrio Francesca Munari Michael Assfalg |
| author_facet | Mariapina D’Onofrio Francesca Munari Michael Assfalg |
| author_sort | Mariapina D’Onofrio |
| collection | DOAJ |
| description | Alpha-synuclein (αS) is an extensively studied protein due to its involvement in a group of neurodegenerative disorders, including Parkinson′s disease, and its documented ability to undergo aberrant self-aggregation resulting in the formation of amyloid-like fibrils. In dilute solution, the protein is intrinsically disordered but can adopt multiple alternative conformations under given conditions, such as upon adsorption to nanoscale surfaces. The study of αS-nanoparticle interactions allows us to better understand the behavior of the protein and provides the basis for developing systems capable of mitigating the formation of toxic aggregates as well as for designing hybrid nanomaterials with novel functionalities for applications in various research areas. In this review, we summarize current progress on αS-nanoparticle interactions with an emphasis on the conformational plasticity of the biomolecule. |
| first_indexed | 2024-03-10T14:27:40Z |
| format | Article |
| id | doaj.art-ea2be020ddaf489eb6c48c2b820b88dc |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T14:27:40Z |
| publishDate | 2020-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-ea2be020ddaf489eb6c48c2b820b88dc2023-11-20T22:52:47ZengMDPI AGMolecules1420-30492020-11-012523562510.3390/molecules25235625Alpha-Synuclein—Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational PlasticityMariapina D’Onofrio0Francesca Munari1Michael Assfalg2Department of Biotechnology, University of Verona, 37134 Verona, ItalyDepartment of Biotechnology, University of Verona, 37134 Verona, ItalyDepartment of Biotechnology, University of Verona, 37134 Verona, ItalyAlpha-synuclein (αS) is an extensively studied protein due to its involvement in a group of neurodegenerative disorders, including Parkinson′s disease, and its documented ability to undergo aberrant self-aggregation resulting in the formation of amyloid-like fibrils. In dilute solution, the protein is intrinsically disordered but can adopt multiple alternative conformations under given conditions, such as upon adsorption to nanoscale surfaces. The study of αS-nanoparticle interactions allows us to better understand the behavior of the protein and provides the basis for developing systems capable of mitigating the formation of toxic aggregates as well as for designing hybrid nanomaterials with novel functionalities for applications in various research areas. In this review, we summarize current progress on αS-nanoparticle interactions with an emphasis on the conformational plasticity of the biomolecule.https://www.mdpi.com/1420-3049/25/23/5625alpha-synucleinamyloid fibrilsconformational flexibilityprotein adsorptionprotein aggregationnano-bio interface |
| spellingShingle | Mariapina D’Onofrio Francesca Munari Michael Assfalg Alpha-Synuclein—Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity Molecules alpha-synuclein amyloid fibrils conformational flexibility protein adsorption protein aggregation nano-bio interface |
| title | Alpha-Synuclein—Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity |
| title_full | Alpha-Synuclein—Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity |
| title_fullStr | Alpha-Synuclein—Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity |
| title_full_unstemmed | Alpha-Synuclein—Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity |
| title_short | Alpha-Synuclein—Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity |
| title_sort | alpha synuclein nanoparticle interactions understanding controlling and exploiting conformational plasticity |
| topic | alpha-synuclein amyloid fibrils conformational flexibility protein adsorption protein aggregation nano-bio interface |
| url | https://www.mdpi.com/1420-3049/25/23/5625 |
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