The interactions between two heme proteins myoglobin (HMb) and horseradish peroxidase (HRP) with zinc oxide (ZnO) nanoparticles are investigated by using UV–vis absorption, steady state fluorescence, synchronous fluorescence, time-resolved fluorescence, FT-IR, atomic force microscopy (AFM) and circular dichroism (CD) techniques under physiological condition of pH∼7.4. The presence of mainly static mode in fluorescence quenching mechanism of HMb and HRP by ZnO nanoparticle indicates the possibility of formation of ground state complex. The processes of bindings of ZnO nanoparticles with the two proteins are spontaneous molecular interaction procedures. In both cases hydrogen bonding plays a major role. The circular dichroism (CD) spectra reveal that a helicity of the proteins is reduced by increasing ZnO nanoparticle concentration although the α-helical structures of HMb and HRP retain their identity. On binding to the ZnO nanoparticles the secondary structure of HRP molecules (or HMb molecules) remains unchanged while there is a substantial change in the environment of the tyrosin active site in case of HRP molecules and tryptophan active site in case of HMb molecules. Tapping mode atomic force microscopy (AFM) was applied for the investigation the structure of HRP adsorbed in the environment of nanoparticles on the silicon and on the bare silicon. HRP molecules adsorb and aggregate on the mica with ZnO nanoparticle. The aggregation indicates an attractive interaction among the adsorbed molecules. The molecules are randomly distributed on the bare silicon wafer. The adsorption of HRP in the environment of ZnO nanoparticle changes drastically the domains due to a strong interaction between HRP and ZnO nanoparticles. Similar situation is observed in case of HMb molecules. These findings demonstrate the efficacy of biomedical applications of ZnO nanoparticles as well as in elucidating their mechanisms of action as drugs in both human and plant systems.
Skip Nav Destination
Article navigation
15 July 2011
Research Article|
July 29 2011
Mode of bindings of zinc oxide nanoparticles to myoglobin and horseradish peroxidase: A spectroscopic investigations
Gopa Mandal;
Gopa Mandal
Department of Spectroscopy Indian Association for the Cultivation of Science Jadavpur
, Kolkata 700032, India
Search for other works by this author on:
Sudeshna Bhattacharya;
Sudeshna Bhattacharya
Department of Spectroscopy Indian Association for the Cultivation of Science Jadavpur
, Kolkata 700032, India
Search for other works by this author on:
Tapan Ganguly
Tapan Ganguly
a)
Department of Spectroscopy Indian Association for the Cultivation of Science Jadavpur
, Kolkata 700032, India
Search for other works by this author on:
a)
Author to whom correspondence should be addressed. Electronic addresses: [email protected] and [email protected].
J. Appl. Phys. 110, 024701 (2011)
Article history
Received:
February 23 2011
Accepted:
June 11 2011
Citation
Gopa Mandal, Sudeshna Bhattacharya, Tapan Ganguly; Mode of bindings of zinc oxide nanoparticles to myoglobin and horseradish peroxidase: A spectroscopic investigations. J. Appl. Phys. 15 July 2011; 110 (2): 024701. https://doi.org/10.1063/1.3610446
Download citation file:
Pay-Per-View Access
$40.00
Sign In
You could not be signed in. Please check your credentials and make sure you have an active account and try again.
Citing articles via
A step-by-step guide to perform x-ray photoelectron spectroscopy
Grzegorz Greczynski, Lars Hultman
Piezoelectric thin films and their applications in MEMS: A review
Jinpeng Liu, Hua Tan, et al.
Tutorial: Simulating modern magnetic material systems in mumax3
Jonas J. Joos, Pedram Bassirian, et al.
Related Content
Quantum-chemical analysis of paramagnetic 13 C NMR shifts of iron-bound cyanide ions in heme-protein environments
AIP Conference Proceedings (December 2012)
Probing the nature of electron transfer in metalloproteins on graphene-family materials as nanobiocatalytic scaffold using electrochemistry
AIP Advances (March 2015)
Experiments with proteins at low temperature: What do we learn on properties in their functional state?
J. Chem. Phys. (April 2007)
Calculation of the circular dichroism spectra of carbon monoxy- and deoxy myoglobin: Interpretation of a time-resolved circular dichroism experiment
J. Chem. Phys. (November 2005)
Vibrational dynamics of thiocyanate and selenocyanate bound to horse heart myoglobin
J. Chem. Phys. (June 2014)