The effect of aluminum oxide on red blood cell integrity and hemoglobin structure at nanoscale

Sharareh Kahbasi; Mahsa Samadbin; Farnoosh Attar; Masomeh Heshmati; Daryoush Danaei; Behnam Rasti; Abbas Salihi; Nadir Mustafa Qadir Nanakali; Falah Mohammad Aziz; Keivan Akhtari; Anwarul Hasan; Mojtaba Falahati

doi:10.1016/j.ijbiomac.2019.07.154

The effect of aluminum oxide on red blood cell integrity and hemoglobin structure at nanoscale

Sharareh Kahbasi, Mahsa Samadbin, Farnoosh Attar, Masomeh Heshmati, Daryoush Danaei, Behnam Rasti, Abbas Salihi, Nadir Mustafa Qadir Nanakali, Falah Mohammad Aziz, Keivan Akhtari, Anwarul Hasan^*, Mojtaba Falahati

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

Abstract

Herein, we explored the interaction of Al₂O₃ NPs with RBCs and Hb to determine the effect of Al₂O₃ NPs on hemolytic activity and Hb denaturation. The percentage of hemolysis of extracts and direct contact assays triggered by Al₂O₃ NPs was calculated by determining supernatant Hb concentration at 540 nm. Far-UV CD and Trp/ANS/acrylamide fluorescence spectroscopic methods were used to determine the structural changes of Hb upon interaction with Al₂O₃ NPs. Theoretical studies were carried out to display the residues involved in the binding site of Hb with Al₂O₃ nanocluster as well as the structural changes of Hb after interaction. The results showed that the percentage of hemolysis of extract and direct contact assays induced by Al₂O₃ NPs were 1.16 and 0.46, respectively. Fluorescence spectroscopy revealed that Al₂O₃ NPs alter the quaternary structure of the protein; however, CD spectroscopy indicated that the secondary structure of Hb remains almost unchanged. Theoretical study displayed that Al₂O₃ nanocluster interacts with different residues of protein, and Hb tends to be destabilized at the binding site with nanocluster. This study may be significant in exploring the toxicity profile of Al₂O₃ NPs for their in vivo implementations.

Original language	English
Pages (from-to)	800-809
Number of pages	10
Journal	International Journal of Biological Macromolecules
Volume	138
DOIs	https://doi.org/10.1016/j.ijbiomac.2019.07.154
State	Published - 1 Oct 2019
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2019

Keywords

Aluminum oxide
Hemoglobin structure
Hemolysis
Nanoparticles
Spectroscopy
Theoretical studies
Toxicity

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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10.1016/j.ijbiomac.2019.07.154

Cite this

Kahbasi, S., Samadbin, M., Attar, F., Heshmati, M., Danaei, D., Rasti, B., Salihi, A., Nanakali, N. M. Q., Aziz, F. M., Akhtari, K., Hasan, A., & Falahati, M. (2019). The effect of aluminum oxide on red blood cell integrity and hemoglobin structure at nanoscale. International Journal of Biological Macromolecules, 138, 800-809. https://doi.org/10.1016/j.ijbiomac.2019.07.154

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title = "The effect of aluminum oxide on red blood cell integrity and hemoglobin structure at nanoscale",

abstract = "Herein, we explored the interaction of Al2O3 NPs with RBCs and Hb to determine the effect of Al2O3 NPs on hemolytic activity and Hb denaturation. The percentage of hemolysis of extracts and direct contact assays triggered by Al2O3 NPs was calculated by determining supernatant Hb concentration at 540 nm. Far-UV CD and Trp/ANS/acrylamide fluorescence spectroscopic methods were used to determine the structural changes of Hb upon interaction with Al2O3 NPs. Theoretical studies were carried out to display the residues involved in the binding site of Hb with Al2O3 nanocluster as well as the structural changes of Hb after interaction. The results showed that the percentage of hemolysis of extract and direct contact assays induced by Al2O3 NPs were 1.16 and 0.46, respectively. Fluorescence spectroscopy revealed that Al2O3 NPs alter the quaternary structure of the protein; however, CD spectroscopy indicated that the secondary structure of Hb remains almost unchanged. Theoretical study displayed that Al2O3 nanocluster interacts with different residues of protein, and Hb tends to be destabilized at the binding site with nanocluster. This study may be significant in exploring the toxicity profile of Al2O3 NPs for their in vivo implementations.",

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AU - Samadbin, Mahsa

AU - Attar, Farnoosh

AU - Heshmati, Masomeh

AU - Danaei, Daryoush

AU - Rasti, Behnam

AU - Salihi, Abbas

AU - Nanakali, Nadir Mustafa Qadir

AU - Aziz, Falah Mohammad

AU - Akhtari, Keivan

AU - Hasan, Anwarul

AU - Falahati, Mojtaba

PY - 2019/10/1

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N2 - Herein, we explored the interaction of Al2O3 NPs with RBCs and Hb to determine the effect of Al2O3 NPs on hemolytic activity and Hb denaturation. The percentage of hemolysis of extracts and direct contact assays triggered by Al2O3 NPs was calculated by determining supernatant Hb concentration at 540 nm. Far-UV CD and Trp/ANS/acrylamide fluorescence spectroscopic methods were used to determine the structural changes of Hb upon interaction with Al2O3 NPs. Theoretical studies were carried out to display the residues involved in the binding site of Hb with Al2O3 nanocluster as well as the structural changes of Hb after interaction. The results showed that the percentage of hemolysis of extract and direct contact assays induced by Al2O3 NPs were 1.16 and 0.46, respectively. Fluorescence spectroscopy revealed that Al2O3 NPs alter the quaternary structure of the protein; however, CD spectroscopy indicated that the secondary structure of Hb remains almost unchanged. Theoretical study displayed that Al2O3 nanocluster interacts with different residues of protein, and Hb tends to be destabilized at the binding site with nanocluster. This study may be significant in exploring the toxicity profile of Al2O3 NPs for their in vivo implementations.

AB - Herein, we explored the interaction of Al2O3 NPs with RBCs and Hb to determine the effect of Al2O3 NPs on hemolytic activity and Hb denaturation. The percentage of hemolysis of extracts and direct contact assays triggered by Al2O3 NPs was calculated by determining supernatant Hb concentration at 540 nm. Far-UV CD and Trp/ANS/acrylamide fluorescence spectroscopic methods were used to determine the structural changes of Hb upon interaction with Al2O3 NPs. Theoretical studies were carried out to display the residues involved in the binding site of Hb with Al2O3 nanocluster as well as the structural changes of Hb after interaction. The results showed that the percentage of hemolysis of extract and direct contact assays induced by Al2O3 NPs were 1.16 and 0.46, respectively. Fluorescence spectroscopy revealed that Al2O3 NPs alter the quaternary structure of the protein; however, CD spectroscopy indicated that the secondary structure of Hb remains almost unchanged. Theoretical study displayed that Al2O3 nanocluster interacts with different residues of protein, and Hb tends to be destabilized at the binding site with nanocluster. This study may be significant in exploring the toxicity profile of Al2O3 NPs for their in vivo implementations.

KW - Aluminum oxide

KW - Hemoglobin structure

KW - Hemolysis

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KW - Spectroscopy

KW - Theoretical studies

KW - Toxicity

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JF - International Journal of Biological Macromolecules

ER -

The effect of aluminum oxide on red blood cell integrity and hemoglobin structure at nanoscale

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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