Publication result detail

Spectral analysis of human norepinephrine transporter homing peptides

HADDAD, Y.; MILOSAVLJEVIĆ, V.; NEJDL, L.; RICHTERA, L.; HEGER, Z.; ADAM, V.

Original Title

Spectral analysis of human norepinephrine transporter homing peptides

English Title

Spectral analysis of human norepinephrine transporter homing peptides

Type

Paper in proceedings (conference paper)

Original Abstract

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.

English abstract

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.

Keywords

UV spectrometry; peptide; tyrosine; tryptophan; targeted therapy

Key words in English

UV spectrometry; peptide; tyrosine; tryptophan; targeted therapy

Authors

HADDAD, Y.; MILOSAVLJEVIĆ, V.; NEJDL, L.; RICHTERA, L.; HEGER, Z.; ADAM, V.

RIV year

2019

Released

31.12.2017

ISBN

978-80-7509-529-9

Book

MendelNet 2017

Pages from

867

Pages to

872

Pages count

6

BibTex

@inproceedings{BUT148725,
  author="Yazan Abdulmajeed Eyadh {Haddad} and Vedran {Milosavljević} and Lukáš {Nejdl} and Lukáš {Richtera} and Zbyněk {Heger} and Vojtěch {Adam}",
  title="Spectral analysis of human norepinephrine transporter homing peptides",
  booktitle="MendelNet 2017",
  year="2017",
  pages="867--872",
  isbn="978-80-7509-529-9"
}

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