Abstract
The binding of silver nanoparticles to bovine hemoglobin (BHb) was studied by fluorescence, UV–Visible, and circular dichroism (CD) spectroscopic techniques at different temperatures of 20, 37, and 42 °C. The absorption spectrum of soret band, in the presence of silver nanoparticle, showed a significant spectral change, which indicated the heme groups of BHb were directly attacked and degraded by silver nanoparticle. The fluorescence data explained that the nanoparticle binding to BHb occurred at a single binding site, which demonstrated a dynamic quenching procedure. Nanoparticles could reduce the fluorescence of tryptophanyl residues of BHb to a lesser extent. Circular dichroism studies demonstrated a conformational change of BHb in the presence of silver nanoparticles. The helicity of BHb was reduced by increasing silver nanoparticle concentration at different temperatures. Thermodynamic analysis of the protein interaction by silver nanoparticles suggested that the binding process is only entropy driven.
Similar content being viewed by others
References
Bao XY, Zhu ZW, Li NQ et al (2001) Electrochemical studies of rutin interacting with hemoglobin and determination of hemoglobin. Talanta 54:591–596. doi:10.1016/S0039-9140(00)00667-6
Barone PW, Baik S, Heller DA et al (2005) Near-infrared optical sensors based on single-walled carbon nanotubes. Nat Mater 4:86–92. doi:10.1038/nmat1276
Besteman K, Lee JO, Wiertz FGM et al (2003) Enzyme-coated carbon nanotubes as single-molecule biosensors. Nano Lett 3:727–730. doi:10.1021/nl034139u
Chaplin MF, Bucke C (1990) Enzyme technology. Cambridge University Press, Cambridge, pp 1–40
Chen X, Schluesener HJ (2008) Silver nanoparticle: a nanoproduct in medical application. Toxicol Lett 176:1–12. doi:10.1016/j.toxlet.2007.10.004
Hong R, Fischer NO, Verma A et al (2004) Control of protein structure and function through surface recognition by tailored nanoparticle scaffolds. J Am Chem Soc 126:739–743. doi:10.1021/ja037470o
Hu YJ, Liu Y, Shen XS, et al (2005) Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin. J Mol Struct 143–147. doi:10.1016/j.molstruc.2004.11.062
Jeong SH, Hwang YH, Yi SC (2005) Antibacterial properties of padded PP/PE nonwovens incorporating nano-sized silver. J Mater Sci 40:5413–5418. doi:10.1007/s10853-005-4340-2
Kandagal PB, Ashoka S, Seetharamappa J et al (2006) Study of the interaction of an anticancer drug with human and bovine serum albumin: spectroscopic approach. J Pharm Biomed 41:393–399. doi:10.1016/j.jpba.2005.11.037
Karajanagi SS, Vertegel AA, Kane RS et al (2004) Structure and function of enzymes adsorbed onto single-walled carbon nanotubes. Langmuir 20:11594–11599. doi:10.1021/la047994h
Loo C, Hirsch L, Lee MH et al (2005) Gold nanoshell bioconjugates for molecular imaging in living cells. Opt Lett 30:1012–1014. doi:10.1364/OL.30.001012
Luckarift HR, Spain JC, Naik RR et al (2004) Enzyme immobilization in a biomimetic silica support. Nat Biotechnol 22:211–213. doi:10.1038/nbt931
Luk YY, Tingey ML, Hall DJ et al (2003) Using liquid crystals to amplify protein-receptor interactions: design of surfaces with nanometer-scale topography that present histidine-tagged protein receptors. Langmuir 19:1671–1680. doi:10.1021/la026152k
Mandal R, Kalke R, Li XF (2004) Interaction of oxaliplatin, cisplatin, and carboplatin with hemoglobin and the resulting release of a heme group. Chem Res Toxicol 17:1391–1397. doi:10.1021/tx049868j
Medintz IL, Uyeda HT, Goldman ER et al (2005) Quantum dot bioconjugates for imaging, labelling and sensing. Nat Mater 4:435–446. doi:10.1038/nmat1390
Messori L, Gabbianii C, Casini A et al (2006) The reaction of artemisinins with hemoglobin: a unified picture. Bioorg Med Chem 14:2972–2977. doi:10.1016/j.bmc.2005.12.038
Mohanpuria P, Rana NK, Yadav SK (2008) Biosynthesis of nanoparticles: technological concepts and future applications. J Nanopart Res 10:507–517. doi:10.1007/s11051-007-9275-x
Niemeyer CM (2001) Nanoparticles, proteins, and nucleic acids: biotechnology meets materials science. Angew Chem Int Ed 40:4128–4158. doi:10.1002/1521-3773(20011119)40:22<4128::AID-ANIE4128>3.0.CO;2-S
Pantarotto D, Briand JP, Prato M, et al (2004) Translocation of bioactive peptides across cell membranes by carbon nanotubes. Chem Commun (Camb) 16–17. doi:10.1039/b311254c
Park SJ, Lazarides AA, Mirkin CA et al (2001) Directed assembly of periodic materials from protein and oligonucleotide-modified nanoparticle building blocks. Angew Chem Int Ed 40:2909–2912. doi:10.1002/1521-3773(20010803)40:15<2909::AID-ANIE2909>3.0.CO;2-O
Patolsky F, Lieber CM (2005) Nanowire nanosensors. Mater Today 8:20–28. doi:10.1016/S1369-7021(05)00791-1
Pender MJ, Sowards LA, Hartgerink JD et al (2006) Peptide-mediated formation of single-wall carbon nanotube composites. Nano Lett 6:40–44. doi:10.1021/nl051899r
Peng X, Manna L, Yang WD et al (2000) Shape control of CdSe nanocrystals. Nature 404:59–61. doi:10.1038/35003535
Roach P, Farrar D, Perry CC (2006) Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry. J Am Chem Soc 128:3939–3945. doi:10.1021/ja056278e
Scheller FW, Bistolas N, Liu SQ et al (2005) Thirty years of haemoglobin electrochemistry. Adv Colloid Interface 116:111–120. doi:10.1016/j.cis.2005.05.006
Shi Kam NW, Jessop TC, Wender PA et al (2004) Nanotube molecular transporters: internalization of carbon nanotubeprotein conjugates into mammalian cells. J Am Chem Soc 126:6850–6851. doi:10.1021/ja0486059
Strano MS, Dyke CA, Usrey ML et al (2003) Electronic structure control of single-walled carbon nanotube functionalization. Science 301:1519–1522. doi:10.1126/science.1087691
Sukdeb P, Yu KT, Joon MS (2007) Does the antibacterial activity of silver nanoparticles depend on the shape of the nanoparticle? A study of the Gram-negative bacterium Escherichia coli. Appl Environ Microbiol 73:1712–1720. doi:10.1128/AEM.02218-06
Tang JH, Luan F, Chen XG et al (2006) Binding analysis of glycyrrhetinic acid to human serum albumin: Fluorescence spectroscopy, FTIR and molecular modeling. Bioorg Med Chem 14:3210–3217. doi:10.1016/j.bmc.2005.12.034
Tao L, Jun Z, Xin G et al (2003) Wiring electrons of cytochrome c with silver nanoparticles in layered films. ChemPhysChem 4:1364–1366. doi:10.1002/cphc.200300817
Xin G, Tao L, Jun Z et al (2004a) Effect of silver nanoparticles on the electron transfer reactivity and the catalytic activity of myoglobin. ChemBioChem 5:1686–1691. doi:10.1002/cbic.200400080
Xin G, Tao L, Xiaoli Z et al (2004b) An electrochemical biosensor for nitric oxide based on silver nanoparticles and hemoglobin. Anal Sci 20:1271–1275. doi:10.2116/analsci.20.1271
Acknowledgments
The financial support given by the University of Tehran is gratefully acknowledged. The authors are also grateful to A. Javed, Department of Biochemistry, University of Agriculture, Faisalabad, Pakistan, for the English editing.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Zolghadri, S., Saboury, A.A., Golestani, A. et al. Interaction between silver nanoparticle and bovine hemoglobin at different temperatures. J Nanopart Res 11, 1751–1758 (2009). https://doi.org/10.1007/s11051-008-9538-1
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11051-008-9538-1