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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.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Kahbasi S,Samadbin M,Attar F,Heshmati M,Danaei D,Rasti B,Salihi A,Nanakali NMQ,Aziz FM,Akhtari K,Hasan A,Falahati M

doi

10.1016/j.ijbiomac.2019.07.154

subject

Has Abstract

pub_date

2019-10-01 00:00:00

pages

800-809

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(19)34465-4

journal_volume

138

pub_type

杂志文章

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