Interactions of human hemoglobin with charged ligand-functionalized iron oxide nanoparticles and effect of counterions
Source abstract
Abstract
Human hemoglobin is an important metalloprotein. It has tetrameric structure with each subunit containing a ‘heme’ group which carries oxygen and carbon dioxide in blood. In this work, we have investigated the interactions of human hemoglobin (Hb) with charged ligand-functionalized iron oxide nanoparticles and the effect of counterions, in aqueous medium. Several techniques like DLS and ζ-potential measurements, UV–vis, fluorescence, and CD spectroscopy have been used to characterize the interaction. The nanoparticle size was measured to be in the range of 20–30 nm. Our results indicated the binding of Hb with both positively as well as negatively charged ligand-functionalized iron oxide nanoparticles in neutral aqueous medium which was driven by the electrostatic and the hydrophobic interactions. The electrostatic binding interaction was not seen in phosphate buffer at pH 7.4. We have also observed that the ‘heme’ groups of Hb remained unaffected on binding with charged nanoparticles, suggesting the utility of the charged ligand-functionalized nanoparticles in biomedical applications.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Protein Interaction Studies and Fluorescence Analysis · Nanoparticle-Based Drug Delivery · Hemoglobin structure and function
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (30)
Show source-provided references
1. Bajaj A, Miranda OR, Kim IB, Phillips RL, Jerry DJ, Bunz UHF, Rotello VM (2009) Detection and differentiation of normal, cancerous, and metastatic cells using nanoparticle-polymer sensor arrays. Proc Natl Acad Sci USA 106:10912–1091610.1073/pnas.0900975106 ↗
2. Cao YC (2008) Nanomaterials for biomedical applications. Nanomedicine 3:467–46910.2217/17435889.3.4.467 ↗
3. Chen K, Xu Y, Rana S, Miranda OR, Dubin PL, Rotello VM, Sun L, Guo X (2011) Electrostatic selectivity in protein-nanoparticle interactions. Biomacromolecules 12:2552–256110.1021/bm200374e ↗
4. De M, Ghosh PS, Rotello VM (2008) Applications of nanoparticles in biology. Adv Mater 20:4225–424110.1002/adma.200703183 ↗
5. Fang C, Zhang M (2009) Multifunctional magnetic nanoparticles for medical imaging applications. J Mater Chem 19:6258–626610.1039/b902182e ↗
6. Garabagiu S (2011) A spectroscopic study on the interaction between gold nanoparticles and hemoglobin. Mater Res Bull 46:2474–247710.1016/j.materresbull.2011.08.032 ↗
7. Ghosh G, Panicker L, Ningthoujam RS, Barick KC, Tewari R (2013) Counter ion induced irreversible denaturation of hen egg white lysozyme upon electrostatic interaction with iron oxide nanoparticles: a predicted model. Colloids Surf B 103:267–27410.1016/j.colsurfb.2012.10.034 ↗
8. Ghosh G, Panicker L, Barick KC (2014a) Selective binding of proteins on functional nanoparticles via reverse charge parity model: an in vitro study. Mater Res Express 1(1–7):01501710.1088/2053-1591/1/1/015017 ↗
9. Ghosh G, Panicker L, Barick KC (2014b) Protein nanoparticle electrostatic interaction: size dependent counterions induced conformational change of hen egg white lysozyme. Colloids Surf B 118:1–610.1016/j.colsurfb.2014.03.026 ↗
10. Lakowicz JR (2006) Principles of fluorescence spectroscopy, 3rd edn. Springer, New York10.1007/978-0-387-46312-4 ↗
11. Laurent S, Forge D, Port M, Roch A, Robic C, Elst IV, Muller RN (2008) Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications. Chem Rev 108:2064–211010.1021/cr068445e ↗
12. Linse S, Cabaleiro-Lago C, Xue WF, Lynch I, Lindman S, Thulin E, Radford SE, Dawson KA (2007) Nucleation of protein fibrillation by nanoparticles. Proc Natl Acad Sci USA 104:8691–869610.1073/pnas.0701250104 ↗
13. Lynch I, Cedervall T, Lundqvist M, Cabaleiro-Lago C, Linse S, Dawson KA (2007) The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century. Adv Colloid Interface Sci 134–135:167–17410.1016/j.cis.2007.04.021 ↗
14. Mahato M, Pal P, Tah B, Ghosh M, Talapatro GB (2011) Study of silver nanoparticle-hemoglobin interaction and composite formation. Colloids Surf B 88:141–14910.1016/j.colsurfb.2011.06.024 ↗
15. Milani S, Bombelli FB, Pitek AS, Dawson KA, Rädler J (2012) Reversible versus irreversible binding of transferrin to polystyrene nanoparticles: soft and hard corona. ACS Nano 6:2532–254110.1021/nn204951s ↗
16. Miranda OR, You CC, Philips R, Kim IB, Ghosh PS, Bunz UHF, Rotello VM (2007) Array-based sensing of proteins using conjugated polymers. J Am Chem Soc 129:9856–985710.1021/ja0737927 ↗
17. Monopoli MP, Åberg C, Salvati A, Dawson KA (2012) Biomolecular coronas provide the biological identity of nanosized materials. Nat Nanotechnol 7:779–78610.1038/nnano.2012.207 ↗
18. Neely A, Perry C, Varisli B, Singh AK, Arbneshi T, Senapati D, Kalluri JR, Ray PC (2009) Ultrasensitive and highly selective detection of Alzheimer’s disease biomarker using two-photon Rayleigh scattering properties of gold nanoparticle. ACS Nano 3:2834–284010.1021/nn900813b ↗
19. Nel AE, Mädler L, Velegol D, Xia T, Hoek EMV, Somasundaran P, Klaessig F, Castranova V, Thompson M (2009) Understanding biophysicochemical interactions at the nano-bio interface. Nat Mater 8:543–55710.1038/nmat2442 ↗
20. Pankhurst QA, Connolly J, Jones SK, Dobson J (2003) Applications of magnetic nanoparticles in biomedicine. J Phys D Appl Phys 36:R167–R18110.1088/0022-3727/36/13/201 ↗
21. Phillips RL, Miranda OR, You CC, Rotello VM, Bunz UHF (2008) Rapid and efficient identification of bacteria using gold-nanoparticle-poly(para-phenyleneethynylene) constructs. Angew Chem Int Ed 7:2590–259410.1002/anie.200703369 ↗
22. Salvati A, Pitek AS, Monopoli MP, Prapainop K, Bombelli FB, Hristov DR, Kelly PM, Åberg C, Mahon E, Dawson KA (2013) Transferrin-functionalized nanoparticles lose their targeting capabilities when a biomolecule corona adsorbs on the surface. Nat Nanotechnol 8:137–14310.1038/nnano.2012.237 ↗
23. Sengupta B, Sengupta PK (2002) The interaction of Quercetin with Human Serum Albumin: a fluorescence spectroscopic study. Biochem Biophys Res Commun 299:400–40310.1016/S0006-291X(02)02667-0 ↗
24. Shang W, Nuffer JH, Muniz-Papandrea VA, Colon W, Siegel RW, Dordick JS (2009) Cytochrome C on silica nanoparticles: influence of nanoparticle size on protein structure, stability, and activity. Small 5:470–47610.1002/smll.200800995 ↗
25. Sokolov L, Mukherji I (2000) Structure of sickle cell hemoglobin fibers probed with UV Resonance Raman spectroscopy. J Phys Chem B 104:10835–1084310.1021/jp000488q ↗
26. Sun W, Wang D, Zhai Z, Gao R, Jiao K (2009) Direct electrochemistry of hemoglobin immobilized in the sodium alginate and SiO2 nanoparticles biocomposite film on a carbon ionic liquid electrode. J Iran Chem Soc 6:412–41910.1007/BF03245852 ↗
27. Wang B, Zhang L, Bae SC, Granick S (2008) Nanoparticle-induced surface reconstruction of phospholipid membranes. Proc Natl Acad Sci USA 105:18171–1817510.1073/pnas.0807296105 ↗
28. Wang YQ, Zhang HM, Zhou QH, Xu HL (2009) A study of the binding of colloidal Fe3O4 with bovine hemoglobin using optical spectroscopy. Colloids Surf A 337:102–10810.1016/j.colsurfa.2008.12.003 ↗
29. Xu Y, Zheng Y, Fan JS, Yang D (2006) A new strategy for structure determination of large proteins in solution without deuteration. Nat Methods 3:931–93710.1038/nmeth938 ↗
30. Zolghadri S, Saboury AA, Amin E, Moosavi-Movahedi AA (2010) A spectroscopic study on the interaction between ferric oxide nanoparticles and human hemoglobin. J Iran Chem Soc 7:S145–S15310.1007/BF03246193 ↗