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Updated: Dec 24, 2025
Protein Kinase C-delta Inhibitor Peptide Formulation using Gold Nanoparticles
Published on: March 9, 2019
Effects of gold nanoparticle morphologies on interactions with proteins
Gongke Wang1, Wanli Wang2, Enbo Shangguan1
1School of Chemistry and Chemical Engineering, Key Laboratory of Green Chemical Media and Reactions, Ministry of Education, Collaborative Innovation Center of Henan Province for Green Manufacturing of Fine Chemicals, Henan Normal University, Xinxiang, Henan 453007, PR China; School of Materials Science and Engineering, Henan Normal University, Xinxiang, Henan 453007, PR China.
Nanoparticle shape significantly impacts protein corona formation and aggregation. Irregularly shaped gold nanoparticles (AuNPs) induce greater changes in protein structure than nanospheres, influencing their biological identity.
Area of Science:
- Nanomedicine
- Biomaterials Science
- Surface Chemistry
Background:
- Nanoparticles interact with biological systems by forming a protein corona, altering their identity and biological fate.
- Understanding protein corona formation is crucial for predicting nanoparticle biodistribution, toxicity, and applications.
- The influence of nanoparticle morphology on protein corona characteristics remains an active area of research.
Purpose of the Study:
- To investigate the effect of gold nanoparticle (AuNP) shape on protein corona structure and function.
- To explore how different protein structures influence AuNP stability and aggregation.
- To establish structure-property relationships between AuNP morphology, protein corona, and nanoparticle behavior.
Main Methods:
- Synthesis of three distinct AuNP morphologies: nanospheres (AuNSPs), nanorods (AuNRs), and nanostars (AuNSs).
- Characterization of protein structure changes using circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR).
- Assessment of AuNP stability and aggregation influenced by protein adsorption using UV-vis spectroscopy, transmission electron microscopy (TEM), microscale thermophoresis (MST), and dynamic light scattering (DLS).
Main Results:
- Irregularly shaped AuNPs (AuNRs, AuNSs) induced more significant alterations in protein secondary structures compared to AuNSPs.
- AuNP shape had a pronounced effect on trypsin (Try) secondary structure and a milder effect on fibrinogen (FIB) secondary structure.
- Protein adsorption and AuNP aggregation were found to be dependent on both AuNP shape and protein type.
Conclusions:
- Nanoparticle morphology is a critical determinant in protein corona formation and subsequent protein structural changes.
- The specific shape of AuNPs influences their interaction with different proteins, affecting protein structure and stability.
- These findings highlight the importance of considering nanoparticle shape in designing nanomaterials for biomedical applications to control biological interactions.
