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Article: Amyloid Protein-Induced Supramolecular Self-Assembly of Water-Soluble Platinum(II) Complexes: A Luminescence Assay for Amyloid Fibrillation Detection and Inhibitor Screening

TitleAmyloid Protein-Induced Supramolecular Self-Assembly of Water-Soluble Platinum(II) Complexes: A Luminescence Assay for Amyloid Fibrillation Detection and Inhibitor Screening
Authors
Issue Date2019
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
Citation
Journal of the American Chemical Society, 2019, v. 141 n. 46, p. 18570-18577 How to Cite?
AbstractAmyloid fibrillation has been acknowledged as a hallmark of a number of neurodegenerative ailments such as Alzheimer’s disease. Accordingly, efficient detection of amyloid fibrillation will allow for great advances in the field of biomedical applications as well as in achieving early medical diagnosis. In this work, a luminescence assay for the sensitive and specific detection of amyloid fibrillation was developed by using platinum(II) complexes as sensing platforms. Supramolecular self-assembly of platinum(II) complexes was induced upon addition of amyloid, leading to alterations in the spectroscopic and luminescence properties of the complexes. As compared to fluorescent dyes, luminescent platinum(II) complexes exhibit attractive large Stokes shifts, phosphorescence lifetimes in the microsecond to submicrosecond regime, and low-energy red emission after aggregation, which are advantageous to biological imaging. At the same time, the platinum(II) complex adopted herein was found to have high photostability, high selectivity and specificity, and low cytotoxicity. The proposed design is the very first approach to detect amyloid fibrillation through the supramolecular self-assembly of luminescent platinum(II) complexes.
Persistent Identifierhttp://hdl.handle.net/10722/285439
ISSN
2023 Impact Factor: 14.4
2023 SCImago Journal Rankings: 5.489
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLaw, ASY-
dc.contributor.authorLee, LCC-
dc.contributor.authorYeung, MCL-
dc.contributor.authorLo, KKW-
dc.contributor.authorYam, VWW-
dc.date.accessioned2020-08-18T03:53:25Z-
dc.date.available2020-08-18T03:53:25Z-
dc.date.issued2019-
dc.identifier.citationJournal of the American Chemical Society, 2019, v. 141 n. 46, p. 18570-18577-
dc.identifier.issn0002-7863-
dc.identifier.urihttp://hdl.handle.net/10722/285439-
dc.description.abstractAmyloid fibrillation has been acknowledged as a hallmark of a number of neurodegenerative ailments such as Alzheimer’s disease. Accordingly, efficient detection of amyloid fibrillation will allow for great advances in the field of biomedical applications as well as in achieving early medical diagnosis. In this work, a luminescence assay for the sensitive and specific detection of amyloid fibrillation was developed by using platinum(II) complexes as sensing platforms. Supramolecular self-assembly of platinum(II) complexes was induced upon addition of amyloid, leading to alterations in the spectroscopic and luminescence properties of the complexes. As compared to fluorescent dyes, luminescent platinum(II) complexes exhibit attractive large Stokes shifts, phosphorescence lifetimes in the microsecond to submicrosecond regime, and low-energy red emission after aggregation, which are advantageous to biological imaging. At the same time, the platinum(II) complex adopted herein was found to have high photostability, high selectivity and specificity, and low cytotoxicity. The proposed design is the very first approach to detect amyloid fibrillation through the supramolecular self-assembly of luminescent platinum(II) complexes.-
dc.languageeng-
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html-
dc.relation.ispartofJournal of the American Chemical Society-
dc.titleAmyloid Protein-Induced Supramolecular Self-Assembly of Water-Soluble Platinum(II) Complexes: A Luminescence Assay for Amyloid Fibrillation Detection and Inhibitor Screening-
dc.typeArticle-
dc.identifier.emailYam, VWW: wwyam@hku.hk-
dc.identifier.authorityYam, VWW=rp00822-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/jacs.9b09515-
dc.identifier.pmid31709796-
dc.identifier.scopuseid_2-s2.0-85074949340-
dc.identifier.hkuros313044-
dc.identifier.volume141-
dc.identifier.issue46-
dc.identifier.spage18570-
dc.identifier.epage18577-
dc.identifier.isiWOS:000499738700028-
dc.publisher.placeUnited States-
dc.identifier.issnl0002-7863-

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