Interactions of ultrashort laser pulses with hemoglobin: Photophysical aspects and potential applications

Radmilović, Mihajlo D.; Drvenica, Ivana; Rabasović, Mihailo D.; Ilić, Vesna; Pavlović, Danica; Oasa, Sho; Vukojević, Vladana; Perić, Mina; Nikolić, Stanko N.; Krmpot, Aleksandar J.

doi:10.1016/j.ijbiomac.2023.125312

Cited by 6 publications

(1 citation statement)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The intrinsic fluorescence of hemoglobin is due to the presence of tryptophans and tyrosines in protein core [14,15] or heme moiety [16]. The main contribution to the intensity of tryptophan UV fluorescence of hemoglobin is Trp37 located at the interface of two αß dimers [14], and the detected signal is sensitive to changes in the tertiary structure of the protein, as well as to ligand binding [15].…”

Section: Evaluation Of Changes In Tryptophan Fluorescence Spectra Dur...mentioning

confidence: 99%

Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation

Kuleshova,

Zaripov,

Poluektov

et al. 2023

IJMS

View full text Add to dashboard Cite

Hemoglobin is the main protein of red blood cells that provides oxygen transport to all cells of the human body. The ability of hemoglobin to bind the main low-molecular-weight thiol of the cell glutathione, both covalently and noncovalently, is not only an important part of the antioxidant protection of red blood cells, but also affects its affinity for oxygen in both cases. In this study, the properties of oxyhemoglobin in complex with reduced glutathione (GSH) and properties of glutathionylated hemoglobin bound to glutathione via an SS bond were characterized. For this purpose, the methods of circular dichroism, Raman spectroscopy, infrared spectroscopy, tryptophan fluorescence, differential scanning fluorimetry, and molecular modeling were used. It was found that the glutathionylation of oxyhemoglobin caused changes in the secondary structure of the protein, reducing the alpha helicity, but did not affect the heme environment, tryptophan fluorescence, and the thermostability of the protein. In the noncovalent complex of oxyhemoglobin with reduced glutathione, the secondary structure of hemoglobin remained almost unchanged; however, changes in the heme environment and the microenvironment of tryptophans, as well as a decrease in the protein’s thermal stability, were observed. Thus, the formation of a noncovalent complex of hemoglobin with glutathione makes a more significant effect on the tertiary and quaternary structure of hemoglobin than glutathionylation, which mainly affects the secondary structure of the protein. The obtained data are important for understanding the functioning of glutathionylated hemoglobin, which is a marker of oxidative stress, and hemoglobin in complex with GSH, which appears to deposit GSH and release it during deoxygenation to increase the antioxidant protection of cells.

show abstract

Section: Evaluation Of Changes In Tryptophan Fluorescence Spectra Dur...mentioning

confidence: 99%

Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation

Kuleshova,

Zaripov,

Poluektov

et al. 2023

IJMS

View full text Add to dashboard Cite

show abstract

Optimization of graphene-based biosensor design for haemoglobin detection using the gradient boosting algorithm for behaviour prediction

Wekalao,

Prasad Srinivasan,

Patel

et al. 2025

Measurement

View full text Add to dashboard Cite

Light on abnormal red blood cell subpopulations: Label-free optics-based approach for studying in vitro rigidified blood cells

Radmilović,

Ilić,

Vučetić

et al. 2025

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

View full text Add to dashboard Cite

Interactions of ultrashort laser pulses with hemoglobin: Photophysical aspects and potential applications

Cited by 6 publications

References 45 publications

Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation

Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation

Optimization of graphene-based biosensor design for haemoglobin detection using the gradient boosting algorithm for behaviour prediction

Light on abnormal red blood cell subpopulations: Label-free optics-based approach for studying in vitro rigidified blood cells

Contact Info

Product

Resources

About