Characterization of Hemoglobin Variants by Capillary Electrophoresis, UV-Vis, and FTIR Spectroscopy
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00064203%3A_____%2F25%3A10489820" target="_blank" >RIV/00064203:_____/25:10489820 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11130/25:10489820
Result on the web
<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=aULJMxo6s-" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=aULJMxo6s-</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/elps.202400154" target="_blank" >10.1002/elps.202400154</a>
Alternative languages
Result language
angličtina
Original language name
Characterization of Hemoglobin Variants by Capillary Electrophoresis, UV-Vis, and FTIR Spectroscopy
Original language description
Hemoglobinopathies, hereditary disorders affecting the structure or production of hemoglobin, were detected by routine HbA(1c) measurements by capillary electrophoresis (CE) at the University Hospital Motol, Prague. The potential of ultraviolet-visible (UV-Vis) and Fourier-transform infrared (FTIR) spectroscopy for the detection and characterization of hemoglobinopathies was investigated. FTIR spectra were recorded with a very high resolution (0.5 cm(-1)) with 128 scans. The broad amide I peak, located at 1700-1600 cm(-1), can be formed by superimposition of the conformational structures of hemoglobin. These secondary protein structures were subjected to mathematical analysis. The application of band narrowing techniques, followed by curve fitting and integration processes, provided the basis for the quantitative estimation of protein secondary structure. As a result, unambiguous differences in UV-Vis spectra among patients with presumably normal hemoglobin, an HbC or a hemoglobin S/hemoglobin G (HbS/HbG)-Philadelphia variant could not be demonstrated. However, FTIR spectra indicated slight differences in α-helix, β-turns, β-sheet, or random coil secondary hemoglobin structures for these mutations. In the spectral wavenumber range of 950-850 cm(-1), there were some obvious FTIR differences at specific wavenumbers between patients with normal hemoglobin and those with the HbC variant. Further investigations are needed with a sufficient number of hemoglobin variants to elucidate the potency of FTIR spectroscopy for the characterization of hemoglobinopathies.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30100 - Basic medicine
Result continuities
Project
—
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Electrophoresis
ISSN
0173-0835
e-ISSN
1522-2683
Volume of the periodical
46
Issue of the periodical within the volume
16
Country of publishing house
DE - GERMANY
Number of pages
9
Pages from-to
1165-1173
UT code for WoS article
001391025000001
EID of the result in the Scopus database
2-s2.0-85214446116