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http://repositorio.ugto.mx/handle/20.500.12059/5093Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.rights.license | http://creativecommons.org/licenses/by-nc-nd/4.0 | es_MX |
| dc.creator | Kayla Young | - |
| dc.date.accessioned | 2021-06-02T15:54:11Z | - |
| dc.date.available | 2021-06-02T15:54:11Z | - |
| dc.date.issued | 2018-11-26 | - |
| dc.identifier.uri | http://repositorio.ugto.mx/handle/20.500.12059/5093 | - |
| dc.description.abstract | La causa de la enfermedad neurodegenerativa conocida como la enfermedad de Alzheimer involucra la agregación de péptidos β-amiloide en el cerebro. Las investigaciones demuestran que el buckminsterfullereno tiene la capacidad de inhibir esta agregación, proporcionando una oportunidad para un tratamiento preventivo a la enfermedad. Aunque se han explorado las cualidades inhibidoras y las interacciones entre esta molécula de carbono y el amiloide, hay información limitada sobre las interacciones de la proteína con monoaductos de fullereno que permiten que la molécula sea soluble en agua y por lo tanto es más aplicable como un tratamiento potencial. Esta investigación profundiza en esta área de interés con la dinámica molecular, que involucró el uso de programas como GROMACS y Grace. Las simulaciones sugieren que los monoaductos de fullereno probados posiblemente tenía un efecto obstaculizaba sobre las protofibrillas del amiloide y su agregación. | es_MX |
| dc.language.iso | eng | es_MX |
| dc.publisher | Universidad de Guanajuato | es_MX |
| dc.relation | http://www.jovenesenlaciencia.ugto.mx/index.php/jovenesenlaciencia/article/view/2610 | - |
| dc.rights | info:eu-repo/semantics/openAccess | es_MX |
| dc.source | Jóvenes en la Ciencia: Verano de la Investigación Científica. Vol. 4, Num 1 (2018) | es_MX |
| dc.title | Simulations of interactions between fullerene monoadducts and β-amyloid protofibrils via molecular dynamics | es_MX |
| dc.type | info:eu-repo/semantics/article | es_MX |
| dc.subject.cti | info:eu-repo/classification/cti/3 | es_MX |
| dc.subject.keywords | Alzheimer’s Disease | es_MX |
| dc.subject.keywords | Modeling | es_MX |
| dc.subject.keywords | Buckminsterfullerene | es_MX |
| dc.subject.keywords | Peptide aggregation | es_MX |
| dc.type.version | info:eu-repo/semantics/publishedVersion | es_MX |
| dc.creator.two | Shariqah Hossain | - |
| dc.creator.three | SUSANA FIGUEROA GERSTENMAIER | - |
| dc.creator.idthree | info:eu-repo/dai/mx/cvu/77409 | es_MX |
| dc.description.abstractEnglish | The cause of the neurodegenerative illness known as Alzheimer’s Disease involves the aggregation of β-amyloid peptides in the brain. Research shows that the buckminsterfullerene has the ability to inhibit this aggregation, providing an opportunity for a preventative treatment to the disease. Although the inhibiting qualities and interactions between this carbon molecule and the amyloid have been explored, there is limited information on the protein ́s interactions with fullerene monoadducts that allow the molecule to be soluble in water and therefore more applicable as a potential treatment. This research delves into this area of interest with Molecular Dynamics, which involved the use of programs such as GROMACS and Grace. The simulations suggest that the the tested fullerene monoadducts had a possible hindering effect on the amyloid protofibrils and their aggregation. | - |
| Appears in Collections: | Revista Jóvenes en la Ciencia | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Simulations of interactions between fullerene monoadducts and β-amyloid protofibrils via molecular dynamics.pdf | 563.45 kB | Adobe PDF | View/Open |
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