Binding of Lanthanide Complexes to Histidine-Containing Peptides Probed by Raman Optical Activity Spectroscopy

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00491276" target="_blank" >RIV/61388963:_____/18:00491276 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22340/18:43916389

Výsledek na webu

<a href="http://dx.doi.org/10.1002/chem.201800840" target="_blank" >http://dx.doi.org/10.1002/chem.201800840</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/chem.201800840" target="_blank" >10.1002/chem.201800840</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Binding of Lanthanide Complexes to Histidine-Containing Peptides Probed by Raman Optical Activity Spectroscopy

Popis výsledku v původním jazyce

Lanthanide complexes are used as convenient spectroscopic probes for many biomolecules. Their binding to proteins is believed to be enhanced by the presence of histidine, but the strength of the interaction significantly varies across different systems. To understand the role of peptide length and sequence, short histidine-containing peptides have been synthesized (His-Gly, His-Gly-Gly, His-Gly-Gly-Gly, Gly-His, Gly-His-Gly, His-His, and Gly-Gly-His) and circularly polarized luminescence (CPL) induced at the [Eu(dpa)(3)](3-) complex has been measured by means of a Raman optical activity (ROA) spectrometer. The obtained data indicate relatively weak binding of the histidine residue to the complex, with a strong participation of other parts of the peptide. Longer peptides, low pH, and a histidine residue close to the N-peptide terminus favor the binding. The binding strengths are approximately proportional to the CPL intensity and roughly correlate with predictions based on molecular dynamics (MD) simulations. The specificity of lanthanide binding to the peptide structure and its intense luminescence and high optical activity make the ROA/CPL technique suitable for probing secondary and tertiary structures of peptides and proteins.

Název v anglickém jazyce

Binding of Lanthanide Complexes to Histidine-Containing Peptides Probed by Raman Optical Activity Spectroscopy

Popis výsledku anglicky

Lanthanide complexes are used as convenient spectroscopic probes for many biomolecules. Their binding to proteins is believed to be enhanced by the presence of histidine, but the strength of the interaction significantly varies across different systems. To understand the role of peptide length and sequence, short histidine-containing peptides have been synthesized (His-Gly, His-Gly-Gly, His-Gly-Gly-Gly, Gly-His, Gly-His-Gly, His-His, and Gly-Gly-His) and circularly polarized luminescence (CPL) induced at the [Eu(dpa)(3)](3-) complex has been measured by means of a Raman optical activity (ROA) spectrometer. The obtained data indicate relatively weak binding of the histidine residue to the complex, with a strong participation of other parts of the peptide. Longer peptides, low pH, and a histidine residue close to the N-peptide terminus favor the binding. The binding strengths are approximately proportional to the CPL intensity and roughly correlate with predictions based on molecular dynamics (MD) simulations. The specificity of lanthanide binding to the peptide structure and its intense luminescence and high optical activity make the ROA/CPL technique suitable for probing secondary and tertiary structures of peptides and proteins.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

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

2018

Kód důvěrnosti údajů

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

Název periodika

Chemistry - A European Journal

ISSN

0947-6539

e-ISSN

—

Svazek periodika

24

Číslo periodika v rámci svazku

34

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

6

Strana od-do

8664-8669

Kód UT WoS článku

000435772200026

EID výsledku v databázi Scopus

2-s2.0-85047484146