1. Graphene quantum dots (GQDs) can interact with human serum albumin (HSA) and cause structural damage.
2. GQDs quench the intrinsic fluorescence of HSA via static mode and bind mainly to site I of HSA.
3. The interaction between GQDs and HSA is mainly through van der Waals interactions and hydrogen bonding interactions, with protonation also playing a role.
The article titled "Study on the molecular interaction of graphene quantum dots with human serum albumin: Combined spectroscopic and electrochemical approaches" provides a detailed investigation of the potential toxicity risk of graphene quantum dots (GQDs) on human health. The study aims to determine whether GQDs could bind and alter the structure and function of human serum albumin (HSA), which is the most important carrier protein in the circulatory system.
The article presents a thorough quantitative and qualitative investigation of the interaction between GQDs and HSA, using spectroscopic and electrochemical approaches. The results show that GQDs could quench the intrinsic fluorescence of HSA via static mode, indicating that they bind to HSA. The binding site of GQDs was mainly located in site I of HSA, as revealed by competitive binding fluorescence assay. Some thermodynamic parameters suggested that GQDs interacted with HSA mainly through van der Waals interactions and hydrogen bonding interactions, and protonation might also participate in the process.
However, the article has some potential biases and missing points of consideration. Firstly, it does not provide enough evidence for its claims regarding the potential toxicity risk of GQDs on human health. While it is mentioned that Nurunnabi et al. studied the in vivo biodistribution and potential toxicity of GQDs for the first time, their results revealed that carboxylated GQDs did not cause appreciable toxicity to treated animals. This suggests that further research is needed to determine whether other types of GQDs may pose a risk to human health.
Additionally, while the article notes that HSA contributes significantly to colloid osmotic blood pressure and participates in transportation, distribution, and metabolism of drugs and nanoparticles, it does not explore how these factors may affect or be affected by GQD-HSA interaction. This limits our understanding of how this interaction may impact drug delivery or nanoparticle distribution in the body.
Furthermore, the article does not present both sides equally. While it provides evidence for the potential toxicity risk of GQDs on human health, it does not explore potential benefits or applications of GQDs in biological and biomedical fields. This one-sided reporting may lead to a biased view of GQDs and their potential impact on human health.
In conclusion, while the article provides valuable insights into the binding mechanism of GQDs with HSA and their potential toxicity risk, it has some biases and missing points of consideration that limit our understanding of this interaction. Further research is needed to determine whether other types of GQDs may pose a risk to human health and how this interaction may impact drug delivery or nanoparticle distribution in the body.