Inner-View of Nanomaterial Incited Protein Conformational Changes: Insights into Designable Interaction

Abstract

<jats:p>Nanoparticle bioreactivity critically depends upon interaction between proteins and nanomaterials (NM). The formation of the “protein corona” (PC) is the effect of such nanoprotein interactions. PC has a wide usage in pharmaceuticals, drug delivery, medicine, and industrial biotechnology. Therefore, a detailed in-vitro, in-vivo, and in-silico understanding of nanoprotein interaction is fundamental and has a genuine contemporary appeal. NM surfaces can modify the protein conformation during interaction, or NMs themselves can lead to self-aggregations. Both phenomena can change the whole downstream bioreactivity of the concerned nanosystem. The main aim of this review is to understand the mechanistic view of NM-protein interaction and recapitulate the underlying physical chemistry behind the formation of such complicated macromolecular assemblies, to provide a critical overview of the different models describing NM induced structural and functional modification of proteins. The review also attempts to point out the current limitation in understanding the field and highlights the future scopes, involving a plausible proposition of how artificial intelligence could be aided to explore such systems for the prediction and directed design of the desired NM-protein interactions.</jats:p>

Gold nanoparticle‐adjuvanted S protein induces a strong antigen‐specific IgG response against severe acute respiratory syndrome‐related coronavirus infection, but fails to induce protective antibodies and limit eosinophilic infiltration in lungs

“…Indeed, AuNP‐adjuvanted S protein induced strong IgG responses to S protein itself in this study; however, it failed to induce protective immune responses and to limit eosinophilic infiltrations after virus challenge. One explanation for the failure to induce protective immune responses could be that structural changes in S protein upon binding to the AuNP adjuvant resulted in S‐binding IgGs that were unable to neutralize the virus . AuNPs and S protein bind together via electrostatic interactions and S‐protein forms a “protein corona” around AuNPs .…”

“…The protein secondary structure is strongly affected by the surface charge of AuNPs . The particle surface of a protein corona defines the biological identity of the particle when it is attached to the cell surface in vivo . Thus, even a small modification in S protein structure could impact both negatively and positively on its immunogenicity.…”

Role of Protein in Fungal Biomineralization of Copper Carbonate Nanoparticles

“…The rearrangement of hydrogen bonds involved in this process results in a decrease in the content of helical structures and other conformational changes. 40 Helices with polar and hydrophilic properties are more prone to attach to NP surfaces, 41 which can explain the strong affinity of TPI with CuNPs. The decrease in the percentage of a helices and an increase in b sheets indicated unfolding of TPI during such association with CuNPs.…”

Self-Assembly of Crystalline Vesicles from Nonplanar π-Conjugated Nanocycles

“…The wide range of applications of nanomaterials in the biomedical and optoelectronic fields has promoted the development of nanocarbon technology. [1][2][3] Some typical π-electron conjugated carbon nanostructures, such as fullerenes, carbon nanotubes, graphene, and so on, have shown excellent electrical, photonic, and physical-chemical properties. 4,5 By virtue of the rational design of certain molecular substructures, such as molecular nanocarbon building blocks, a complex and organized supramolecular carbon nanostructure can be formed by molecular self-assembly based on noncovalent interactions of molecular nanocarbons.…”