Table 1.
The table provides the brief information about the different synthesis techniques being followed along with some of the major advantages and disadvantages of each technique
| Technique | Advantage | Disadvantage | References |
|---|---|---|---|
| Solvent extraction/emulsion process |
The rate of encapsulation is very high Require basic laboratory equipment |
Large particle size Poor drug loading Uncontrolled drug release |
[96, 97] |
| Complex Coacervation |
Performed under mild conditions High shell integrity Excellent drug release efficacy |
Agglomeration chances are high Easily affected by temperature, pH, ionic strength, composition, and nature of the material |
[98, 99] |
| Salt precipitation | A simple and robust technique | High chances of confirmation and bioactivity loss | [111] |
| Polyelectrolyte complexation |
Encapsulation efficiency is high Maintains the drug stability |
Affected by pH variations, temperature, ionic strength, polyelectrolyte concentration | [112] |
| Desolvation |
Easy synthesis Low cost High yield |
Protein denaturation Loss of biological activity Affected by the pH of the protein |
[100, 101] |
| Heat denaturation |
Targeting moieties can be attached Implemented on a large scale |
Large particle size Not suggested for heat-sensitive compounds |
[113] |
| UV illumination | Assist in the self-assembly of proteins | Chances of agglomeration | [94] |
| Layer-by-layer assembly |
Multilayered structures Controlled size and surface charge Monodisperse particles Unlimited geometry of protein nanoparticles |
Relatively low yield Computational calculations needed Affected by protein concentration |
[104, 105, 114] |
| Electrohydrodynamic jetting |
The secondary protein structure retained Able to trap hydrophobic and hydrophilic drugs Maintain the narrow dispersity of particles |
Low yield Affected by the molecular weight of the protein |
[102, 103] |
| Solvent extraction/emulsion process |
The rate of encapsulation is very high Require basic laboratory equipment |
Large particle size Poor drug loading Uncontrolled drug release |
[96, 97] |
| Complex Coacervation |
Performed under mild conditions High shell integrity Excellent drug release efficacy |
Agglomeration chances are high Easily affected by temperature, pH, ionic strength, composition, and nature of the material |
[98, 99] |
| Salt precipitation | A simple and robust technique | High chances of confirmation and bioactivity loss | [111] |
| Polyelectrolyte complexation |
Encapsulation efficiency is high Maintains the drug stability |
Affected by pH variations, temperature, ionic strength, polyelectrolyte concentration | [112] |
| Desolvation |
Easy synthesis Low cost High yield |
Protein denaturation Loss of biological activity Affected by the pH of the protein |
[100, 101] |
| Heat denaturation |
Targeting moieties can be attached Implemented on a large scale |
Large particle size Not suggested for heat-sensitive compounds |
[113] |
| UV illumination | Assist in the self-assembly of proteins | Chances of agglomeration | [94] |
| Layer-by-layer assembly |
Multilayered structures Controlled size and surface charge Monodisperse particles Unlimited geometry of protein nanoparticles |
Relatively low yield Computational calculations needed Affected by protein concentration |
[104, 105, 114] |
| Electrohydrodynamic jetting |
The secondary protein structure retained Able to trap hydrophobic and hydrophilic drugs Maintain the narrow dispersity of particles |
Low yield Affected by the molecular weight of the protein |
[102, 103] |