Table 3.
Summary of analytical techniques to conduct physico-chemical characterisation, monitor nanoparticle surface driven protein conformational changes and uptake of nanoparticles by cellular structures
| Analysis of | Analytical technique | Brief description | Ref |
|---|---|---|---|
|
Nanoparticle physical characterisation | |||
| Size and charge |
Dynamic light scattering |
Changes in the hydrodynamic diameter of NP upon binding to proteins |
[1] |
| Analytical Ultracentrifugation |
Changes in the hydrodynamic diameter of NP |
[6] |
|
| Dissolution |
Inductively coupled mass spectrometry |
For detecting elemental composition of the nanomaterial |
[90] |
| Shape and structure |
X ray diffraction |
Determination of crystalline structure |
[38] |
| Electron microscopy |
Visualisation of nanoparticle structure |
||
| Surface area |
Braunauer Emmet Teller method |
Measures specific surface area using adsorption of gas on the surface |
[38] |
| De-agglomeration |
Ultrasonication |
Uses sound energy to disrupt large aggregates of NP |
[36] |
|
Nanoparticle protein interaction | |||
| Protein binding affinity |
Isothermal calorimetry |
To measure binding constant, thermodynamic parameters of NP-protein interactions |
[2] |
| Fluorescence spectroscopy |
Measures change in fluorescence spectra due to NP-protein interaction |
[65] |
|
| UV–vis spectroscopy |
Measures change in absorption spectra due to NP-protein interaction |
[57] |
|
| Quartz crystal balance |
Detects change in mass at the oscillating quartz surface due to NP-protein interaction |
[91] |
|
| Surface Plasmon resonance |
Detects change in oscillation of electrons on a metal surface due to NP-protein interaction |
[92] |
|
| Atomic force microscopy |
Gives surface profile of the nanomaterial |
[93] |
|
| Fluorescence correlation spectroscopy |
Binding characteristics depending on fluctuation in florescence |
[94] |
|
|
Nanoparticle surface induced protein structure changes | |||
| Protein structural changes after binding |
Circular Dichroism spectroscopy |
Measures changes in secondary structure of proteins depending on chiral properties of proteins |
[61] |
| Fourier transformed infrared spectroscopy |
Measures adsorption of amide bonds in the proteins to derive structural change |
[43] |
|
| Raman spectroscopy |
Studies molecular vibrations to predict structure |
[52] |
|
| Nuclear Magnetic Resonance |
Relies on magnetic properties of atomic nuclei to predict structure |
[4] |
|
|
Nanoparticle- Cellular interactions | |||
| NP uptake | Confocal microscopy |
Visualization of fluorescent nanoparticles in vitro | [59] |
| Confocal micro Raman spectroscopy | [95] | ||