journal article·2015-01-14

Breaking of the Phosphodiester Bond: A Key Factor That Induces Hemolysis

Tiantian Wang, Xiue Jiang

Publisher page

Abstract

In-depth understanding the toxicity of nanomaterials in red blood cells (RBCs) is of great interest, because of the importance of RBCs in transporting oxygen in blood circulation. Although the toxic effects of nanoparticles in RBCs have been revealed, the conclusions from the literature are conflicting, and in particular, the toxic mechanism is still at the infant stage. Herein, we investigated the size-dependent toxicity of well-known CdTe semiconductor quantum dots (QDs) and revealed the exact toxic mechanism at the molecular level by confocal microscopy and Fourier transform infrared (FT-IR) spectroscopy techniques. We found that smaller mercaptosuccinic acid-capped CdTe QDs (MSA-QDs) with the green-emitting color could cause hemagglutination whereas the middle-size yellow-emitting MSA-QDs induced the formation of stomatocytes and echinocytes and the bigger size red-emitting MSA-QDs induced heavy hemolysis and the formation of lots of ghost cells. The FT-IR data proved that all the MSA-QDs were likely to bond to the RBCs membranes and caused the structural changes of lipid and protein in RBCs. But only the red-emitting MSA-QDs caused the breakage of the phosphodiester bond, which might cause the heavy hemolysis. To some extent, this is the first example that reveals the hemolysis mechanism at the molecular level.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Protein Interaction Studies and Fluorescence Analysis · Neonatal Health and Biochemistry · Pharmacological Effects and Toxicity Studies

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China

Graduate University of Chinese Academy of Sciences, Beijing 100049, China

Funding

National Natural Science Foundation of China · Chinese Academy of Sciences · Natural Science Foundation of Jilin Province

References (46)

Show source-provided references
1. Asharani P. V. · Adv. Funct. Mater. · 2010 · 20 · 123310.1002/adfm.200901846 ↗
2. Yu T. · ACS Nano · 2011 · 5 · 571710.1021/nn2013904 ↗
3. Zhao Y. · ACS Nano · 2011 · 5 · 136610.1021/nn103077k ↗
4. Choi J. · Toxicol. Sci. · 2011 · 123 · 13310.1093/toxsci/kfr149 ↗
5. Lin Y.-S. · J. Am. Chem. Soc. · 2010 · 132 · 483410.1021/ja910846q ↗
6. Shi J. · Acta Biomater. · 2012 · 8 · 347810.1016/j.actbio.2012.04.024 ↗
7. Backman L. · J. Cell Sci. · 1986 · 80 · 28110.1242/jcs.80.1.281 ↗
8. Nakao M. · Nature · 1960 · 187 · 94510.1038/187945a0 ↗
9. Nakao M. · J. Biochem. · 1961 · 49 · 48710.1093/oxfordjournals.jbchem.a127333 ↗
10. LaBrake C. C. · Biochemistry · 1993 · 32 · 1029610.1021/bi00090a004 ↗
11. Park Y. K. · Proc. Natl. Acad. Sci. U. S. A · 2010 · 107 · 128910.1073/pnas.0910785107 ↗
12. Liu X. · Nanoscale · 2013 · 5 · 398210.1039/c3nr00284e ↗
13. Slowing I. I. · Small · 2009 · 5 · 5710.1002/smll.200800926 ↗
14. Sovadinova I. · Biomacromolecules · 2011 · 12 · 26010.1021/bm1011739 ↗
15. Chen H.-C. · Biochim. Biophys. Acta, Biomembr. · 2000 · 1468 · 29310.1016/S0005-2736(00)00271-6 ↗
16. Mantsch H. H. · Chem. Phys. Lipids · 1991 · 57 · 21310.1016/0009-3084(91)90077-O ↗
17. Mendelsohn R. · Chem. Phys. Lipids · 1998 · 96 · 14110.1016/S0009-3084(98)00085-1 ↗
18. Moore D. J. · Biochim. Biophys. Acta, Biomembr. · 1999 · 1415 · 34210.1016/S0005-2736(98)00203-X ↗
19. Derenne A. · Analyst · 2012 · 137 · 325510.1039/c2an35116a ↗
20. Jiang W. · Langmuir · 2004 · 20 · 1143310.1021/la049043+ ↗
21. Jiang W. · Langmuir · 2010 · 26 · 1807110.1021/la103738e ↗
22. Petibois C. · Cell Biol. Int. · 2005 · 29 · 70910.1016/j.cellbi.2005.04.007 ↗
23. Rigas B. · Proc. Natl. Acad. Sci. U. S. A. · 1990 · 87 · 814010.1073/pnas.87.20.8140 ↗
24. Wang T. · ACS Nano · 2012 · 6 · 125110.1021/nn203892h ↗
25. Howarth M. · Proc. Natl. Acad. Sci. U. S. A. · 2005 · 102 · 758310.1073/pnas.0503125102 ↗
26. Klostranec J. M. · Adv. Mater. · 2006 · 18 · 195310.1002/adma.200500786 ↗
27. Larson D. R. · Science · 2003 · 300 · 143410.1126/science.1083780 ↗
28. Clift M. J. D. · Toxicol. Appl. Pharmacol. · 2008 · 232 · 41810.1016/j.taap.2008.06.009 ↗
29. Fahmi M. Z. · Nanoscale · 2013 · 5 · 151710.1039/c2nr33429a ↗
30. Kirchner C. · Nano Lett. · 2005 · 5 · 33110.1021/nl047996m ↗
31. Liu Y. F. · Eur. J. Inorg. Chem. · 2010 · 2010 · 150110.1002/ejic.200900978 ↗
32. Bao H. · Small · 2006 · 2 · 47610.1002/smll.200500346 ↗
33. Ying E. · PLoS One · 2008 · 3 · e222210.1371/journal.pone.0002222 ↗
34. Röcker C. · Nat. Nanotechnol. · 2009 · 4 · 57710.1038/nnano.2009.195 ↗
35. Ataka K. · J. Am. Chem. Soc. · 2004 · 126 · 1619910.1021/ja045951h ↗
36. Ataka K. · J. Am. Chem. Soc. · 2003 · 125 · 498610.1021/ja0346532 ↗
37. Ataka K. · J. Am. Chem. Soc. · 2004 · 126 · 944510.1021/ja048346n ↗
38. Rozner S. · Colloids Surf., B · 2010 · 77 · 2210.1016/j.colsurfb.2009.12.026 ↗
39. Petibois C. · J. Lab. Clin. Med. · 2000 · 135 · 21010.1067/mlc.2000.104460 ↗
40. Connor P. A. · Langmuir · 1999 · 15 · 291610.1021/la980894p ↗
41. Petrone L. · J. R. Soc., Interface · 2011 · 8 · 41010.1098/rsif.2010.0316 ↗
42. Parikh S. J. · Langmuir · 2006 · 22 · 849210.1021/la061359p ↗
43. Ibrahim M. · Indian J. Pure Appl. Phys. · 2005 · 43 · 911
44. Torii, H.; Tasumi, M.InInfrared Spectroscopy of Biomolecules;Mantsch, H. H.; Chapman, D., Eds.John Wiley & Sons:New York; 1996; pp1–18.
45. Naumann, D.; Schultz, C. P.; Helm, D.InInfrared Spectroscopy of Biomolecules;Mantsch, H. H.; Chapman, D., Eds.John Wiley & Sons:New York; 1996; pp279–310.
46. Kong J. · Acta Biochim. Biophys. Sin. · 2007 · 39 · 54910.1111/j.1745-7270.2007.00320.x ↗