Induced Lanthanide Circularly Polarized Luminescence as a Probe of Protein Fibrils

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00503693" target="_blank" >RIV/61388963:_____/19:00503693 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15310/19:73594114

Výsledek na webu

<a href="https://pubs.acs.org/doi/full/10.1021/acsomega.8b03175" target="_blank" >https://pubs.acs.org/doi/full/10.1021/acsomega.8b03175</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acsomega.8b03175" target="_blank" >10.1021/acsomega.8b03175</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Induced Lanthanide Circularly Polarized Luminescence as a Probe of Protein Fibrils

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Induced Lanthanide Circularly Polarized Luminescence as a Probe of Protein Fibrils

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

ACS Omega

ISSN

2470-1343

e-ISSN

—

Svazek periodika

4

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

7

Strana od-do

1265-1271

Kód UT WoS článku

000460214700138

EID výsledku v databázi Scopus

2-s2.0-85060169371