Spectral analysis of human norepinephrine transporter homing peptides

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216305%3A26620%2F17%3APU128354" target="_blank" >RIV/00216305:26620/17:PU128354 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/62156489:43210/17:43912624

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Spectral analysis of human norepinephrine transporter homing peptides

Popis výsledku v původním jazyce

UV spectrometry is very simple and cheap method for quantitative and qualitative analysis of compounds. Furthermore, it provides intricate information about the bonded ��-electron transitions and also non-bonded n-electron transitions. The aim of this work was to identify electron transition bands in two homing peptides of the human norepinephrine transporter (hNET); namely: GASNGINAYL (978 Da) and SLWERLAYGI (1206 Da). Electron transition bands directly indicate structural conformations, particularly the ones associated with double bonds, i.e. conjugated ��-bonds of aromatic and peptide bonds. The results show unusual spikes in absorbance in the far UV at low temperature for GASNGINAYL and even more at other temperatures for SLWERLAYGI peptide. The latter supports the hypothesis of a stacking between tyrosine and tryptophan resulting in helix structure. Infrared spectrometry also showed abundant helix structure in SLWERLAYGI but less abundant in GASNGINAYL peptide. Based on ��-stacking, an UV spectrometry method can be developed to monitor the helicity of some peptides, such as SLWERLAYGI.

Název v anglickém jazyce

Spectral analysis of human norepinephrine transporter homing peptides

Popis výsledku anglicky

UV spectrometry is very simple and cheap method for quantitative and qualitative analysis of compounds. Furthermore, it provides intricate information about the bonded ��-electron transitions and also non-bonded n-electron transitions. The aim of this work was to identify electron transition bands in two homing peptides of the human norepinephrine transporter (hNET); namely: GASNGINAYL (978 Da) and SLWERLAYGI (1206 Da). Electron transition bands directly indicate structural conformations, particularly the ones associated with double bonds, i.e. conjugated ��-bonds of aromatic and peptide bonds. The results show unusual spikes in absorbance in the far UV at low temperature for GASNGINAYL and even more at other temperatures for SLWERLAYGI peptide. The latter supports the hypothesis of a stacking between tyrosine and tryptophan resulting in helix structure. Infrared spectrometry also showed abundant helix structure in SLWERLAYGI but less abundant in GASNGINAYL peptide. Based on ��-stacking, an UV spectrometry method can be developed to monitor the helicity of some peptides, such as SLWERLAYGI.

Druh

D - Stať ve sborníku

CEP obor

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OECD FORD obor

10403 - Physical chemistry

Projekt

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Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název statě ve sborníku

MendelNet 2017

ISBN

978-80-7509-529-9

ISSN

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e-ISSN

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Počet stran výsledku

6

Strana od-do

867-872

Název nakladatele

Neuveden

Místo vydání

Neuveden

Místo konání akce

Brno

Datum konání akce

8. 11. 2017

Typ akce podle státní příslušnosti

CST - Celostátní akce

Kód UT WoS článku

000440194500155