Computational Studies about the Interactions of Nanomaterials with Proteins and their Impacts

TL;DR

This paper reviews recent computational studies on how nanomaterials, especially carbon and gold types, interact with proteins, affecting their functions and guiding biomedical applications.

Contribution

It provides a systematic overview of computational insights into nanomaterial-protein interactions, highlighting mechanisms and design implications.

Findings

Interaction modes are influenced by nanomaterial functional groups and coatings.

Nanomaterials can bind multiple proteins, affecting their activity.

Mechanistic understanding aids in designing nanomaterials for biomedical use.

Abstract

Intensive concerns about the biosafety of nanomaterials demand the systematic study of the mechanisms about their biological effects. Many biological effects can be attributed to the interaction of nanomaterials with protein and their impacts on protein function. On the other hand, nanomaterials exhibit the potential in a variety of biomedical applications, many of which also involve the direct interaction with protein. In this paper, we review some recent computational studies about this subject, especially the interaction of carbon and gold nanomaterials. Besides the hydrophobic and {\pi}-stacking interactions, the interaction mode of carbon nanomaterials can be regulated by their functional groups. And the coating of gold nanomaterials also adjusts their interaction mode, in addition to the coordination interaction with cysteine's sulfur group and histidine's imidazole group. Moreover, nanomaterials can interact with multiple proteins and the impacts on protein activity are attributed to a wide spectrum of mechanisms. The findings about the mechanisms of nanomaterial-protein interaction can further guide the design and development of nanomaterial to realize the applications in disease diagnosis and treatment.