journal article·2011-12Open access

Gold nanoparticle induced conformational changes in heme protein

Dibakar Sahoo, Prosenjit Bhattacharya, Hirak Kumar Patra, Paulami Mandal, Sankar Chakravorti

Journal of Nanoparticle Research· Volume 13· Issue 12

Abstract

Change of α-helical structure of heme protein (Hb) to a β-sheet and random coil conformation because of the interaction of glycine capped gold nanoparticles (20–60 nm) as observed from attenuation total reflectance, absorption, Fourier transform infra red, and Circular Dichroism spectroscopy has been reported in this article. Upon interaction, protein takes a cylindrical shape of length 12 μm and diameter 0.35 μm as revealed from scanning electron microscopy and transmission electron microscopy. The Selected-Area Electron beam Diffraction pattern shows change of crystalline structure in GNP to amorphous nature with the interaction of Hb.
Source: openaire · Quality: candidate unverified · Source record ↗

Research context

OpenAlex topics: Hemoglobin structure and function · Photosynthetic Processes and Mechanisms · Protein Interaction Studies and Fluorescence Analysis

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

References (21)

Show source-provided references
1. Acampora G, Hermans J (1967) Reversible denaturation of sperm whale myoglobin. I. Dependence on temperature, pH, and composition. J Am Chem Soc 89:1543–154910.1021/ja00983a001 ↗
2. Adler AJ (1973) Methods in enzymology, vol 27. Academic Press, New York
3. Aubin-Tam ME, Hamad-Schifferli K (2008) Structure and function of nanoparticle–protein conjugates. Biomed Mater 3:034001–03401710.1088/1748-6041/3/3/034001 ↗
4. Bolanos-Garcia VM, Ramos S, Castillo R, Xicohtencatl-Cortes J, Mas-Oliva J (2001) Monolayers of apolipoproteins at the air/water interface. J Phys Chem B 105:5757–576510.1021/jp010714b ↗
5. Brewer SH, Glomm WR, Johnson MC, Knag MK, Franzen S (2005) Probing BSA binding to citrate-coated gold nanoparticles and surfaces. Langmuir 21:9303–930710.1021/la050588t ↗
6. Campas M, Katakis I (2006) Characterisation and determination of stability and functionality of biofunctionalised colloidal gold nanoparticles. Anal Chim Acta 556:306–31210.1016/j.aca.2005.09.032 ↗
7. Chung PH, Perevedentseva E, Tu JS, Chang CC, Cheng LC (2006) Spectroscopic study of bio-functionalized nanodiamonds. Diamond Relat Mater 15:622–62510.1016/j.diamond.2005.11.019 ↗
8. Keating CD, Kovaleski KM, Natan MJ (1998) Protein:colloid conjugates for surface enhanced Raman scattering: stability and control of protein orientation. J Phy Chem B 102:9404–941310.1021/jp982723z ↗
9. Kristinsson HG (2002) Acid-induced unfolding of flounder hemoglobin: evidence for a molten globular state with enhanced pro-oxidative activity. J Agric Food Chem 50:7669–767610.1021/jf0256788 ↗
10. Lin AWH, Lewinski NA, West JL, Halas NJ, Drezek RA (2005) Optically tunable nanoparticle contrast agents for early cancer detection: model-based analysis of gold nanoshells. J Biomed Opt 10:06403510.1117/1.2141825 ↗
11. Li-Ven D, Colthup NB, Fateley WG, Grasselli JG (1991) The hand book of infrared and Raman characteristic frequencies of organic molecules. Academic Press, Boston
12. Matsui M, Nakahara A, Takatsu A, Kato K, Matsuda N (2008) In situ observation of the state and stability of hemoglobin adsorbed onto glass surface by slab optical waveguide (SOWG) spectroscopy. Int J Chem Biomol Eng 1:72–75
13. Nassar AEF, Rusling JF, Nakashima N (1996) Electron transfer between electrodes and heme proteins in protein–DNA films. J Am Chem Soc 118:3043–304410.1021/ja960065v ↗
14. Noronha M, Santos R, Paci E, Santos H, Macanita AL (2009) Fluorescence lifetimes of tyrosine residues in cytochrome C as local probes to study protein unfolding. Phys Chem B 113:4466–447410.1021/jp805781r ↗
15. Quinten M, Kreibig U (1986) Optical properties of aggregates of small metal particles. Surf Sci 172:557–57710.1016/0039-6028(86)90501-7 ↗
16. Rosi NL, Giljohann DA, Thaxton CS, Lytton-Jean AKR, Han MS, Mirkin CA (2006) Oligonucleotide-modified gold nanoparticles for intracellular gene regulation. Science 312:1027–103010.1126/science.1125559 ↗
17. Tu AT (1986) Peptide backbone conformation and microenvironment of protein side chains. In: Clark RJH, Hester RE (eds) Spectroscopy of biological systems, vol 1. Wiley, New York
18. Vigneshwaran N, Kathe AA, Varadarajan PV, Nachane RP, Balasubramanya RH (2007) Silver–protein (core–shell) nanoparticle production using spent mushroom substrate. Langmuir 23:7113–711710.1021/la063627p ↗
19. Wangoo N, Suri CR, Shekhawat G (2008) Interaction of gold nanoparticles with protein: a spectroscopic study to monitor protein conformational changes. Appl Phy Lett 92:133104–13310610.1063/1.2902302 ↗
20. Woody RW (1996) Circular dichroism and conformational analysis of biomolecules. Plenum Press, New York
21. Yang L, Xing RM, Shen QM, Jiang K, Ye F, Wang JY, Ren QS (2006) Fabrication of protein-conjugated silver sulfide nanorods in the bovine serum albumin solution. J Phys Chem B 110:10534–1053910.1021/jp055603h ↗