Establishing the link between fibril formation and Raman optical activity spectra of insulin

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00476008" target="_blank" >RIV/61388963:_____/17:00476008 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/17:10372336

Výsledek na webu

<a href="http://dx.doi.org/10.1039/c7cp01556a" target="_blank" >http://dx.doi.org/10.1039/c7cp01556a</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c7cp01556a" target="_blank" >10.1039/c7cp01556a</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Establishing the link between fibril formation and Raman optical activity spectra of insulin

Popis výsledku v původním jazyce

Folding of proteins into insoluble amyloidal fibrils is implicated in a number of biological processes. Optical spectroscopy represents a convenient tool to monitor such structural variations. Recently, characteristic changes in Raman optical activity (ROA) spectra of insulin during a pre-fibrillar stage were reported but not supported by a theoretical model. In the present study, molecular dynamics and the density functional theory are used to simulate the spectra and understand the connection between the structure, and ROA and Raman spectral intensities. Theoretical results are consistent with the observations and only confirm exceptional ROA sensitivity to the protein tertiary structure. Surprisingly, this sensitivity reflects local conformational changes in the peptide main and side chains, rather than a direct through-space interaction of the protein components. Side chains providing strong ROA signals, such as tyrosine, can additionally report on local conformational features. Theoretical modeling helps in explaining the observed spectral changes and is likely to enable future applications of ROA spectroscopy in protein structural studies.

Název v anglickém jazyce

Establishing the link between fibril formation and Raman optical activity spectra of insulin

Popis výsledku anglicky

Folding of proteins into insoluble amyloidal fibrils is implicated in a number of biological processes. Optical spectroscopy represents a convenient tool to monitor such structural variations. Recently, characteristic changes in Raman optical activity (ROA) spectra of insulin during a pre-fibrillar stage were reported but not supported by a theoretical model. In the present study, molecular dynamics and the density functional theory are used to simulate the spectra and understand the connection between the structure, and ROA and Raman spectral intensities. Theoretical results are consistent with the observations and only confirm exceptional ROA sensitivity to the protein tertiary structure. Surprisingly, this sensitivity reflects local conformational changes in the peptide main and side chains, rather than a direct through-space interaction of the protein components. Side chains providing strong ROA signals, such as tyrosine, can additionally report on local conformational features. Theoretical modeling helps in explaining the observed spectral changes and is likely to enable future applications of ROA spectroscopy in protein structural studies.

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

2017

Kód důvěrnosti údajů

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

Název periodika

Physical Chemistry Chemical Physics

ISSN

1463-9076

e-ISSN

—

Svazek periodika

19

Číslo periodika v rámci svazku

21

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

8

Strana od-do

13614-13621

Kód UT WoS článku

000402488300025

EID výsledku v databázi Scopus

2-s2.0-85024094350