JOURNAL OF APPLIED PHYSICS 109, 034704 2011

Effect of surface adsorbed proteins on the photoluminescence of nanodiamond

E. Perevedentseva,1,2 N. Melnik,1,a C.-Y. Tsai,2 Y.-C. Lin,2 M. Kazaryan,1 and C.-L. Cheng2,b
1 2

P.N. Lebedev Physics Institute, RAS, 119991 Moscow, Russia Department of Physics, National Dong Hwa University, 97401 Hualien, Taiwan

Received 2 September 2010; accepted 9 December 2010; published online 11 February 2011 Nanodiamond has recently attracted great attention for its intrinsic luminescence in the visible range which can be used as a tracking marker in many biological applications. In this work, photoluminescence PL of nanodiamonds interacting with biological macromolecules, such as proteins lysozyme and albumin, is studied. Proteins were physically adsorbed on carboxylated nanodiamonds surfaces. The PL spectra of the protein-nanodiamond complex were measured. It is shown that the surface passivation can modify the nanodiamond luminescence properties. Changes in shape and spectral positions of the nanodiamond PL band were observed and found to depend on excitation wavelength. We attribute the effects to the surface energy traps and transfer between protein and surface nanostructures, particular the graphitelike nanoclusters. This study is important for the bio and medical applications of nanodiamonds used as a biocompatible label. 2011 American Institute of Physics. doi:10.1063/1.3544312
I. INTRODUCTION

Photoluminescence PL of carbon nanostructures, including nanodiamond ND , is recently attracting much attention both in fundamental researches and applications. Particularly, ND is emerging to be a convenient nanomaterial for various biological and medical applications. Using the luminescence properties of NDs for development of nanomarkers,14 nano- and submicron light sources,5,6 etc., has been demonstrated recently, taking advantages of their unique physical/chemical properties, including optical properties. The diamond color center luminescence is stable, does not photobleach, the emission range is broad, and with relatively high intensity, can be excited with different excitation wavelengths. In addition, ND is available in a variety of sizes and the surface properties structure, electric potential is suitable for bioconjugation, and especially, the biocompatibility and noncytotoxicity make ND a preferable nanomaterial in comparison with semiconductor quantum dots.7,8 Although PL of ND is studied extensively for its potential applications as a biocompatible label, despite various efforts, many questions still exist. Diamond is a wide-band gap semiconductor with a variety of luminescent centers associated with structural defects and donor-acceptor pairs.9 The optical properties of ND and diamondlike carbon are directly related to their structure, such as the types of different carbon spx x = 1 3 bonding, the structural phases distribution,10,11 the size of nanocrystallites and nanoclusters,1214 and the types and distribution of bulk and surface defects and admixtures.1518 Other carbon nanostructures have also been an interest of studies, such as
a b

carbon nanotubes and fullerenes and their derivatives;19 the carbon nanostructures have been reported to emit efciently in the visible range. Modication of optical and spectroscopic properties of nanocarbon systems is proposed via surface interactions. For example, new class of uorescent nanoparticles, such as carbon dots, is developed which do not have intrinsic uorescence but whose uorescence arises as a result of surface passivation.20,21 Nanodiamond forming photonics crystals under high-speed centrifugation has been observed.22 PL spectra of fullerenes reveal the fullerene interaction with different solvent mediums.23,24 For bioimaging applications, the methods to increase the uorescence of ND are recently developed. The so-called uorescent ND is prepared via high energy beam treatment, followed by high temperature annealing.2,25 Together with these methods, the modication of nanocarbon and ND systems properties with surface modication/conjugations open wide possibilities for further development of ND applications for nanoprobing and sensing. In the present work, we study the optical properties of NDs with adsorbed proteins on their surfaces. We use a well known model protein, lysozyme, as an example, as well as blood serum albumin, an important substance in the blood system. The proteins were physically adsorbed on the ND particles, and PL spectra of the ND-protein complexes were measured using different excitations wavelengths. The changes in NDs PL after surface passivation with macromolecules is discussed in terms of surface energy traps and transfer between protein and surface nanostructures in the form of graphitelike nanoclusters, defects, etc., on diamond surfaces.
II. EXPERIMENTAL

Electronic mail: melnik@sci.lebedev.ru. Electronic mail: clcheng@mail.ndhu.edu.tw.

Synthetic diamond powders were purchased from Kay Industrial Diamond USA . These NDs were produced using
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high temperature/high pressure HTHP method.26 Samples with three different average sizes of the particles have been used, the sizes accordingly certicate were 100, 300, and 500 nm. The chemical purity was more than 98%, only tenth of a percent of Cl, Ca, Fe, Si, and, even less some other admixtures may be presented, according to the company specication. HTHP synthesized NDs usually have diamond core with some graphite and disordered carbon admixtures existing on the surface. The images of the particles having the shape of the nonregular crystals were obtained with scanning electron microscopy SEM, JEOL JSM6500F . Although nothing was undertaken against the ND aggregation in suspension, the dynamic light scattering DLS measurements with samples in water suspensions DLS, Brookhaven BI200SM, with BI-9000 digital correlator , demonstrated that these relatively large NDs have signicant fraction of separated nanoparticles reaching several tens of percent, together with particles aggregates. The average sizes of single nanoparticles of the three samples, measured with DLS, were about 130, 195, and 580 nm we refer to nominal sizes below . The SEM images not shown here also conrmed the size of the individual diamond nanocrystals well agrees with DLS observation. The as-received NDs were washed using the strong acid treatment with H2SO4 : HNO3 in relation 3:1, for 24 h, at room temperature. Details of the washing method and the spectroscopic characterization have been described previously.2729 The washing removes metallic impurities and nondiamond carbon on the ND surfaces as well as carboxylates or oxidizes the surface creating COOH and some other oxygen-containing surface groups, results in carboxylated ND cND .29 The pH of ND water suspensions was varied with additions of small quantities of NaOH or HCl water solutions and measured with a Sentron pH-meter Titan, Taiwan . Carboxylation is characterized using Fourier transform infrared FTIR spectroscopy with a Bomem 154B FTIR spectrometer Canada ; well-resolved line of C v O stretching of the carbonyl group was observed on the ND surface in the 1720 1780 cm1 range.29 Proteins lysozyme Amresco, USA and albumin Sigma, USA were physically adsorbed on cND via the method described before.27 In short, the proteins were dissolved in deionized water bidistilled water, pH 6 ; the proteins concentrations were in the range of 300350 mM. To estimate the adsorption,27 the protein solutions were checked with UV/visible spectrometer V-550, Jasco, Japan . Since the band maximum intensity is proportional to concentration, a molar absorbance of lysozyme 3.7547 104 M1 cm1 served to calibrate the lysozyme concentration by the measured absorbance at the absorption band maximum at 280 nm, characteristic for the most proteins. The initial concentration of the protein in solution was pre-set at preparation, and absorption spectra were measured before adsorption; then cND was added to the solution with concentration 2 mg/ml. To ensure equilibration of the adsorption, the protein solution and the cND powder were thoroughly mixed together with a shaker for 2 h, after which the mixture was several times centrifuged and washed with deionized water to remove the nonadsorbed protein. After rst separation of

(a) I-1 II
PL Intensity (a.u.)

I-2
Absorbance

III (b) I III

200 300 400 500 600 700 800

II

Wavelength (nm)

FIG. 1. Color online Absorption spectrum I , and emission spectra of proteins lysozyme a and albumin b at 325 nm II and 488 III nm wavelength laser excitations.

cND with adsorbed protein, the absorption spectra were measured again, and the residual concentration of protein in the supernatant was estimated. The amount of adsorbed protein on the cND surface can be estimated by the difference between initial and residual protein concentrations in solution. The adsorption of proteins on ND surface was also veried using FTIR spectroscopy, to ensure the protein molecules are in close contact with the cND surface. The prepared and repeatedly washed suspensions of ND after the interaction with protein were dropped on Si substrate, thoroughly dried and IR spectra were measured using an FTIR spectrometer, FTLA 2000, Bomem, Canada with a DTGS detector. The spectra reveal signicant dominated protein amide I, II peaks at 1655 and 1540 cm1, correspondingly,30 relative to the characteristic peaks of ND particularly, C v O stretching peak of COOH surface groups at 1760 1820 cm1 for 100500 nm NDs .29 It means that signicant quantity of proteins covers the ND surface. The NDs under studied were not exposed to any special high-energy/ thermal annealing treatment to increase the uorescence.25 PL spectra of ND and proteins samples also the Raman spectra were obtained using a confocal micro Raman spectrometer T64000, Jobin Yvon, France with laser excitation wavelengths 532 and 630 nm, and -SNOM Witec, Germany with excitation 488 nm. Throughout the experiments, low laser power, less then 0.5 mW measured in focal spot was used to avoid laser damage both to the proteins and the NDs. The spectra were measured for samples prepared using the same procedure as for the IR measurements, with water suspensions of the cND-protein complexes dropped and dried on Si wafer substrate.
III. RESULTS

In Fig. 1, the absorption spectra of lysozyme a and albumin b solutions are presented I . In Fig. 1 a , the ab-

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Absorbance

III I II IV

200

300

400

500

600

700

800

900

Wavelength (nm)

FIG. 2. Color online Absorption spectra I and emission spectra of 300 nm cND at excitation wavelengths 325 II , 488 III , and 532 IV nm.

sorption is compared before lysozyme adsorption I-1 and after adsorption on the cND I-2, 300 nm cND . Further washing of ND-proteins suspensions and UV-visible absorption spectra conrm that the cND-protein complex is stable and adsorption is strong. FTIR spectroscopic measurements also conrm that signicant quantity of protein covers the ND surface spectra not shown . The proteins emission spectra are also presented in Fig. 1 at different excitations: II for 325 nm wavelength laser excitation and III for 488 nm wavelength excitation. No uorescence/luminescence emission from these proteins was observed at excitation wavelengths from 488 nm and higher, only the Raman spectra of the proteins are observed. Although some emission is observed at UV excitation, the analysis of PL of ND with adsorbed protein excited with visible light is not obstructed by PL signal from the proteins. Figure 2 depicts the absorption and emission luminescence spectra of 300 nm cND. The UV-visible absorption spectrum of 300 nm cND I and emission at excitations 325 II , 488 III , and 532 IV nm are presented together for comparison. Along with the PL of ND, Raman signal from the sample is also observed. Raman peaks of Si substrate 520.7 cm1 and the second order, wide peak centered about 990 cm1 are observed near 500 nm and 513 nm, correspondingly, for 488 nm excitation wavelength; near 547 and 561.5 nm at 532 nm wavelength excitation; near 654.5 and 675 nm at 632 nm wavelength excitation. Diamond Raman peak, centered at 1332 cm1 is observed near 522 nm, 572.5 nm and 691 nm, correspondingly for each of the excitations. At 488 nm wavelength excitation, a wide Raman peak of amorphous carbon near 1350 cm1 or 522.5 nm is also clearly observed. The Raman spectra of pure proteins are well-observed at excitation 488 nm Fig. 1, III but the ad-

sorbed proteins do not exhibit Raman signal strong enough to be observed on the background of the proteins PL at 325 nm wavelength excitation, as well as in the much stronger PL of ND, at other excitation wavelengths. Details of the observed peaks are tabulated in Table I. At the 488 nm wavelength excitation, the luminescence of ND is predominantly excited at 500630 nm attributed to N-V 0 with zero phonon line at 575 nm and H3 defect centers.31 The band near 670680 nm with zero phonon line ZPL at 639 nm is attributed to N-V centers and is predominantly excited at excitation with 514 or 532 nm wavelengths. This band is partly observed also at 633 nm wavelength excitation; as well as at 488 nm it is observed together with predominant line near 500530 nm. PL properties of diamond depend on the crystals origin, treatment, doping, etc. The NDs PL spectrum is very complicate and not all peculiarities are fully attributed although most of the observed PL peaks of different kinds of diamond structures were studied before.18,31 The peak in area 415425 nm probably can be attributed to the N3 center, related to B-aggregates of nitrogen three nearest substitutional nitrogen atoms bonded to a common vacancy ; 496 nm is attributed to the H4 center, it seems to correlate with concentration of the B-aggregates of nitrogen 3N-V-N or the complex 3NV-V-N ; 503 nm and broad band 525 nm are associated with the H3 center, which may decorate single dislocations and may be yielded by strong mechanical deformations; 516 nm 2.40 eV was observed but not described. The center emitting at 737 nm is known as the Si-V defect. Note that the 737 nm PL feature was observed in association with several additional peaks;31 we observe from them peaks near 573.5 nm, 594 nm, series of peaks in the ranges 535539 and 644652 nm. The peak near 880 nm is observed at excitation wavelength of 325 nm; it is the so called 1.4 eV system, the most studied Ni-related center in diamond is the 1.4 eV system, consisting of two ZPL-lines assigned to Ni+ ion in the center of a diamond divacancy, where Ni is probably not bonded to the carbon neighbors.32 In Fig. 3 the effects of adsorbed proteins on the PL spectra of 300 nm ND at different wavelengths of excitation are compared. The maximal effect is observed for PL in the range of 530750 nm at 488 nm wavelength excitation. This wavelength excites PL of ND presumably in the range of 500600 nm the band in the 620750 nm range is also excited but is weaker . In the presence of proteins the band in the 630730 nm range becomes signicantly stronger. At ex-

TABLE I. The silicon and diamond Raman peaks observed together with the PL spectrum at various wavelength excitation wavelengths. Raman peaks cm1 Excitation wavelengths nm 488 532 632 488 532 632 Raman peaks location in PL spectrum nm 500, 547, 654, 513 561 675

Si

520.7,

990

PL Intensity (a.u.)

Diamond C, sp3

1332

522 572,5 690

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(a) I II

(b)

Wave function

Adsorbed Macromolecule

Surface Carbon Nanocluster

Intensity (a.u.)

II
C

Diamond F

F D

(c) I II

(d)

E G

IV I II
600 650

III
Wavelength (nm)
700 750 800 850

500 550 600 650 700 750 800 850

FIG. 3. Color online Comparison of PL spectra of 300 nm cND with and without protein: a , I: 300 nm cND, II: 300 nm cND with adsorbed albumin, excitation wavelength 488 nm; b , I: 300 nm cND, II: 300 nm cND with adsorbed albumin, excitation wavelength 532 nm; c , I: 300 nm cND, II: 300 nm cND with adsorbed lysozyme, excitation wavelength 488 nm; d , I: 300 nm cND, II: 300 nm cND with adsorbed lysozyme, excitation wavelength 532 nm; III: 300 nm cND, IV: 300 nm cND with adsorbed lysozyme, excitation wavelength 633 nm.

FIG. 5. Color online A schematic representation of the energy transfer between ND surface carbon nanocluster, protein molecule, and diamond structure. A: energy ground state; B: excitation; C: excited states of surface carbon nanocluster, where from excitation transfers to D: energy levels of excited states of diamond, provided by defects and admixtures; emission from these states gives wide luminescence band E. F: excited states of surface carbon nanocluster with adsorbed macromolecule; F : energy levels of protein molecule; energy transfers between the nanocluster and macromolecule and between nanocluster and defects and admixtures in diamond structure; the emission from these states gives the shifted luminescence band G. In the experiment, the luminescence is observed as the superposition of G and E, composing band H.

citations by 532 nm and 633 nm wavelengths, only the peak in the 620750 nm range or part of it is excited, and a small redshift and peak widening are observed. Note that other peaks are not modied by proteins adsorption, for example, there was not any effect observed for the peak at 880 nm at excitation wavelength 325 nm data not shown here . In the Fig. 4 the PL spectra of 100 nm and 500 nm cND at 488 nm wavelength excitation are compared. From Figs. 3 and 4 one can see that the inuence of the same adsorbed protein is more signicant for cND of larger sizes.
IV. DISCUSSION

The effect of the protein adsorption on NDs of different size is visible in Figs. 3 a , 3 c , and 4. When the protein is adsorbed on NDs, for all studied sizes, the band in the 630 730 nm range becomes stronger in comparison with the band
(a) (b)

II

II I
500 550 600 650 700 750 800

I
500 550 600 650 700 750 800 850

Wavelength (nm)

FIG. 4. Color online Comparison of PL spectra of 100 nm a and 500 nm b cND; I: cND, II: cND with lysozyme, excitation wavelength 488 nm.

in the 500600 nm range. The relative intensity of the band in the 630730 nm range without adsorbed protein is lower for larger size NDs; while with adsorbed protein, the larger is the ND the more intense is this additional band. However, with the increasing of the particles size, the inuence of the surface should decrease. It means that the contribution of bulk diamond part in the ND PL prevails. The observed effect can be explained in terms of energy transfer between the diamond structure, surface carbon nanocluster, probably with graphitelike structure33,34 and adsorbed protein molecule as shown schematically in Fig. 5 . The surface of ND is always graphitized and contains carbon with nondiamond structure such as disordered graphite, graphene, other sp2 hybridized peculiarities, etc. Some of these structures exist in the form of nanoparticles nanoclusters with narrow bandgap effectively absorbing light.33,34 When the characteristic size of the nanoclusters is less than the effective size of the wave function of the excited electron, this electron can effectively interact with nearest environment of this carbon nanocluster,33,34 diamond core or adsorbed protein molecule. Particularly, this photoexcited electron can pass from surface carbon nanocluster to ND structure and relax in diamond structure on different radiation centers with emission of the photons. Simultaneously, directly excited PL from photoluminescent centers in diamond bulk also takes place. The exciting energy is the same in both cases, and PL spectra also coincide. When protein molecules are adsorbed on the ND surface, the excited electrons from the carbon nanoclusters can tunnel both into diamond bulk and into protein molecule. Some of the excited electrons tunneling in the protein molecule can nonradiatively transfer part of electron energy in the protein molecule, if this energy correlates with energy levels structure of the molecule. Note that the protein mol-

Intensity (a.u.)

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of them can happen due to disordering the surface structure and the forming carbon nanoclusters contributing participating in PL emission.
V. CONCLUSION

Intensity (a.u.)

II I
570 575 580 585

Intensity (a.u.)

t=50 sec
II

II

III

t > 110 sec

III

550

600

650

700

750

800

850

Wavelength (nm)

500

Wavelength (nm)

600

700

800 1200 1600 2000 -1 Wavenumber (cm )

(a)

(b)

FIG. 6. Color online a The PL spectra of 100 nm cND layer on Si substrate . I: before laser treatment; II: after laser treatment with power 20 mW. The spectra are measured using 532 nm wavelength excitation and 1 mW laser power. The inset shows the extended spectra in the range of Raman signal of graphite. b Changes with time of PL spectra of cND layer on Si substrate at 10 mW laser power treatment, and 488 nm wavelength excitation. On the right hand side, the extended spectra in the range of Raman signal of graphite are shown.

The effect of ND surface passivation with protein molecules on PL spectra of ND is observed. The contribution of surface graphitelike nanoclusters into ND PL is discussed. The adsorption of protein molecules affects the ND PL spectra. The effect depends on excitation wavelength, generally, redshifted PL is observed when protein is adsorbed on the ND surfaces. We propose a mechanism involving surface energy traps and transfer between protein, surface graphitelike nanoclusters and diamond bulk structure. It is important for further understanding the complex uorescence spectra of ND used for biolabeling and tracking.
ACKNOWLEDGMENTS

ecule is not luminescent at the excitation wavelengths used. If after that the electron with lower energy tunnels into diamond core with its photoluminescent centers, it can relax with emission of photons. Lower energy of excitation leads to lower energy emission from the ND bulk and appears as the corresponding luminescence peak in the spectrum. As a result, the shift characterizing the appearance of second peak is observed. The distance between initial and appearing peaks is, in general, determined by set of energy states of the protein molecule, so, presumably, from these spectra the information about the electronic state of the molecules can be obtained; however this assumption needs to be studied in more detail. Note that the effect of surface adsorption can vary for different NDs depending on their structure, admixtures, etc. as well as for different adsorbed molecules. The energy loss is determined by interaction of the protein molecule with surface carbon nanocluster, i.e., by protein and nanocluster properties. Different kinds of photoluminescent centers, which can be effectively excited by different excitation wavelengths, predominate in ND of different sizes and different origin.35 The inuence of surface graphitic structures on the PL of ND can be directly observed by comparing the PL from ND sample and from the same sample after the laser treatments with power able to burn the surface 1020 mW, while for measurements power less 1 mW is used , correspondingly, create additional graphitic structures. The graphite itself does not reveal PL. In Fig. 6 for 100 nm cNDs one can see the arising Raman D- and G-bands after laser treatment, while before treatment only the diamond peak was observed. After forming the additional graphitic structures the graphite peaks predominate on the diamond one, rst of all owing to the Raman cross-section for graphite is much higher than for diamond. With graphitization of the surface signicant broadening the PL band Fig. 6 a as well as the increasing of the PL intensity Fig. 6 b are observed. Both

The authors wish to thank the National Science Council of Taiwan for nancially supporting this project under Grant No. NSC-98-2120-M-259-001 and a joint Taiwan-Russia Research Cooperation project Grant No. NSC-97-2923-M259-MY3 between National Science Council and Russian Foundation for Basic Research NSC-RFBR . The work also is particularly supported by Russian Foundation for Basic Research under Grant No. 10-02-00809-a.
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