Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid
The structural transformation producing amyloids is a phenomenon that sheds new light on the protein folding problem. The analysis of the polymorphic structures of the α-synuclein amyloid available in the PDB database allows analysis of the amyloid-oriented structural transformation itself, but also...
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MDPI AG
2023-04-01
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| Online Access: | https://www.mdpi.com/2227-9059/11/5/1324 |
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| author | Irena Roterman Katarzyna Stapor Leszek Konieczny |
| author_facet | Irena Roterman Katarzyna Stapor Leszek Konieczny |
| author_sort | Irena Roterman |
| collection | DOAJ |
| description | The structural transformation producing amyloids is a phenomenon that sheds new light on the protein folding problem. The analysis of the polymorphic structures of the α-synuclein amyloid available in the PDB database allows analysis of the amyloid-oriented structural transformation itself, but also the protein folding process as such. The polymorphic amyloid structures of α-synuclein analyzed employing the hydrophobicity distribution (fuzzy oil drop model) reveal a differentiation with a dominant distribution consistent with the micelle-like system (hydrophobic core with polar shell). This type of ordering of the hydrophobicity distribution covers the entire spectrum from the example with all three structural units (single chain, proto-fibril, super-fibril) exhibiting micelle-like form, through gradually emerging examples of local disorder, to structures with an extremely different structuring pattern. The water environment directing protein structures towards the generation of ribbon micelle-like structures (concentration of hydrophobic residues in the center of the molecule forming a hydrophobic core with the exposure of polar residues on the surface) also plays a role in the amyloid forms of α-synuclein. The polymorphic forms of α-synuclein reveal local structural differentiation with a common tendency to accept the micelle-like structuralization in certain common fragments of the polypeptide chain of this protein. |
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| issn | 2227-9059 |
| language | English |
| last_indexed | 2024-03-11T03:56:12Z |
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| spelling | doaj.art-eca32d197dae4e269136ce7a8a9b051f2023-11-18T00:35:23ZengMDPI AGBiomedicines2227-90592023-04-01115132410.3390/biomedicines11051324Structural Specificity of Polymorphic Forms of α-Synuclein AmyloidIrena Roterman0Katarzyna Stapor1Leszek Konieczny2Department of Bioinformatics and Telemedicine, Jagiellonian University—Medical College, Medyczna 7, 30-688 Krakow, PolandDepartment of Applied Informatics, Silesian University of Technology, Akademicka 2A, 44-100 Gliwice, PolandMedical Biochemistry, Jagiellonian University—Medical College, Kopernika 7, 31-034 Krakow, PolandThe structural transformation producing amyloids is a phenomenon that sheds new light on the protein folding problem. The analysis of the polymorphic structures of the α-synuclein amyloid available in the PDB database allows analysis of the amyloid-oriented structural transformation itself, but also the protein folding process as such. The polymorphic amyloid structures of α-synuclein analyzed employing the hydrophobicity distribution (fuzzy oil drop model) reveal a differentiation with a dominant distribution consistent with the micelle-like system (hydrophobic core with polar shell). This type of ordering of the hydrophobicity distribution covers the entire spectrum from the example with all three structural units (single chain, proto-fibril, super-fibril) exhibiting micelle-like form, through gradually emerging examples of local disorder, to structures with an extremely different structuring pattern. The water environment directing protein structures towards the generation of ribbon micelle-like structures (concentration of hydrophobic residues in the center of the molecule forming a hydrophobic core with the exposure of polar residues on the surface) also plays a role in the amyloid forms of α-synuclein. The polymorphic forms of α-synuclein reveal local structural differentiation with a common tendency to accept the micelle-like structuralization in certain common fragments of the polypeptide chain of this protein.https://www.mdpi.com/2227-9059/11/5/1324α-synucleinamyloidmisfoldingexternal force fieldhydrophobic core |
| spellingShingle | Irena Roterman Katarzyna Stapor Leszek Konieczny Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid Biomedicines α-synuclein amyloid misfolding external force field hydrophobic core |
| title | Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid |
| title_full | Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid |
| title_fullStr | Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid |
| title_full_unstemmed | Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid |
| title_short | Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid |
| title_sort | structural specificity of polymorphic forms of α synuclein amyloid |
| topic | α-synuclein amyloid misfolding external force field hydrophobic core |
| url | https://www.mdpi.com/2227-9059/11/5/1324 |
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