Please use this identifier to cite or link to this item:
https://hdl.handle.net/10316/103331
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ferreira, Elisabete | - |
dc.contributor.author | Almeida, Zaida L. | - |
dc.contributor.author | Cruz, Pedro F. | - |
dc.contributor.author | Sousa, Marta Silva e | - |
dc.contributor.author | Veríssimo, Paula | - |
dc.contributor.author | Brito, Rui M. M. | - |
dc.date.accessioned | 2022-11-07T12:07:09Z | - |
dc.date.available | 2022-11-07T12:07:09Z | - |
dc.date.issued | 2021-12-30 | - |
dc.identifier.issn | 1422-0067 | pt |
dc.identifier.uri | https://hdl.handle.net/10316/103331 | - |
dc.description.abstract | Several degenerative amyloid diseases, with no fully effective treatment, affect millions of people worldwide. These pathologies-amyloidoses-are known to be associated with the formation of ordered protein aggregates and highly stable and insoluble amyloid fibrils, which are deposited in multiple tissues and organs. The disruption of preformed amyloid aggregates and fibrils is one possible therapeutic strategy against amyloidosis; however, only a few compounds have been identified as possible fibril disruptors in vivo to date. To properly identify chemical compounds as potential fibril disruptors, a reliable, fast, and economic screening protocol must be developed. For this purpose, three amyloid fibril formation protocols using transthyretin (TTR), a plasma protein involved in several amyloidoses, were studied using thioflavin-T fluorescence assays, circular dichroism (CD), turbidity, dynamic light scattering (DLS), and transmission electron microscopy (TEM), in order to characterize and select the most appropriate fibril formation protocol. Saturation transfer difference nuclear magnetic resonance spectroscopy (STD NMR) was successfully used to study the interaction of doxycycline, a known amyloid fibril disruptor, with preformed wild-type TTR (TTRwt) aggregates and fibrils. DLS and TEM were also used to characterize the effect of doxycycline on TTRwt amyloid species disaggregation. A comparison of the TTR amyloid morphology formed in different experimental conditions is also presented. | pt |
dc.language.iso | eng | pt |
dc.relation | PTDC/QUI-QUI/122900/2010 | pt |
dc.relation | UID/NEU/04539/2013 | pt |
dc.relation | UID/QUI/00313/2019 | pt |
dc.relation | SFRH/BD/137991/2018 | pt |
dc.relation | FEDER/COMPETE 2020 and FCT grants RECI/QEQ-QFI/0168/2012, UID/QUI/00313/2019, and PINFRA/22161/2016 (PTNMR) | pt |
dc.rights | openAccess | pt |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | pt |
dc.subject | amyloid disruptors; amyloid fibrils; amyloidosis; fibril disaggregation; protein aggregation; screening protocol; transthyretin | pt |
dc.subject.mesh | Amyloid | pt |
dc.subject.mesh | Circular Dichroism | pt |
dc.subject.mesh | Doxycycline | pt |
dc.subject.mesh | Hydrogen-Ion Concentration | pt |
dc.subject.mesh | Nephelometry and Turbidimetry | pt |
dc.subject.mesh | Prealbumin | pt |
dc.subject.mesh | Protein Structure, Secondary | pt |
dc.subject.mesh | Proton Magnetic Resonance Spectroscopy | pt |
dc.subject.mesh | Protein Aggregates | pt |
dc.title | Searching for the Best Transthyretin Aggregation Protocol to Study Amyloid Fibril Disruption | pt |
dc.type | article | - |
degois.publication.firstPage | 391 | pt |
degois.publication.issue | 1 | pt |
degois.publication.title | International Journal of Molecular Sciences | pt |
dc.peerreviewed | yes | pt |
dc.identifier.doi | 10.3390/ijms23010391 | pt |
degois.publication.volume | 23 | pt |
dc.date.embargo | 2021-12-30 | * |
uc.date.periodoEmbargo | 0 | pt |
item.grantfulltext | open | - |
item.fulltext | Com Texto completo | - |
item.openairetype | article | - |
item.languageiso639-1 | en | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
crisitem.author.researchunit | CQC - Coimbra Chemistry Centre | - |
crisitem.author.researchunit | CNC - Center for Neuroscience and Cell Biology | - |
crisitem.author.researchunit | CQC - Coimbra Chemistry Centre | - |
crisitem.author.parentresearchunit | Faculty of Sciences and Technology | - |
crisitem.author.parentresearchunit | Faculty of Sciences and Technology | - |
crisitem.author.orcid | 0000-0003-3578-0134 | - |
crisitem.author.orcid | 0000-0003-0532-4242 | - |
crisitem.author.orcid | 0000-0001-9128-2557 | - |
Appears in Collections: | I&D CQC - Artigos em Revistas Internacionais I&D CNC - Artigos em Revistas Internacionais |
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File | Description | Size | Format | |
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Searching-for-the-best-transthyretin-aggregation-protocol-to-study-amyloid-fibril-disruptionInternational-Journal-of-Molecular-Sciences.pdf | 2.71 MB | Adobe PDF | View/Open |
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