ArticleACS omega2019
Induced Lanthanide Circularly Polarized Luminescence as a Probe of Protein Fibrils.
Article in ACS omega, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
3 citing papers in PubMed.
- Circularly polarized luminescence from Tb(III) interacting with chiral polyether macrocycles.Dalton transactions (Cambridge, England : 2003) · 2022Article
- A Flexible Circularly Polarized Luminescence Switching Device Based on Proton-Coupled Electron Transfer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Chiral Lanthanide Complexes with l- and d-Alanine: An X-ray and Vibrational Circular Dichroism Study.Molecules (Basel, Switzerland) · 2020Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein fibrils are involved in a number of biological processes. Because their structure is very complex and not completely understood, different spectroscopic methods are used to monitor different aspects of fibril structure. We have explored circularly polarized luminescence (CPL) induced in lanthanide compounds to indicate fibril growth and discriminate among fibril types. For hen egg-white lysozyme and polyglutamic acid-specific CPL, spectral patterns were obtained and could be correlated with vibrational circular dichroism (VCD) spectra and thioflavin T fluorescence. The CPL spectra were measured on a Raman optical activity spectrometer, and its various polarization modes are discussed. The experiments indicate that the induced CPL is sensitive to more local aspects of the fibril structure than VCD. For CPL, smaller amounts of the sample are required for the analysis, and thus this method appears to be a good candidate for future spectroscopic characterization of these peptide and protein aggregates.
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Registered trials
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