Molecular dynamics simulations suggest the potential toxicity of fluorinated graphene to HP35 protein via unfolding the α-helix structure

• Published in: Scientific reports Vol. 14; no. 1; p. 9168
• Main Authors: Zou, Fangrong, Gu, Zonglin, Perez-Aguilar, Jose Manuel, Luo, Yuqi
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 22.04.2024; Nature Publishing Group; Nature Portfolio
• Subjects: 631/57/2282; 639/925/928; Adsorption; Denaturation; Electrostatic properties; Fluorinated graphene; Fluorine; Graphene; Graphite - chemistry; Graphite - toxicity; Halogenation; HP35 protein; Humanities and Social Sciences; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Hydrophobicity; Molecular dynamics; Molecular Dynamics Simulation; Molecular modelling; multidisciplinary; Nanomaterials; Nanostructures - chemistry; Nanostructures - toxicity; Nanotechnology; Neurofilament Proteins; Peptide Fragments; Protein Conformation, alpha-Helical; Protein folding; Protein Unfolding - drug effects; Proteins; Science; Science (multidisciplinary); Toxicity; Unfolding; HP35 protein; Unfolding; Molecular dynamics simulation; Toxicity; Fluorinated graphene
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/s41598-024-59780-3

Fluorinated graphene, a two-dimensional nanomaterial composed of three atomic layers, a central carbon layer sandwiched between two layers of fluorine atoms, has attracted considerable attention across various fields, particularly for its potential use in biomedical applications. Nonetheless, scant effort has been devoted to assessing the potential toxicological implications of this nanomaterial. In this study, we scrutinize the potential impact of fluorinated graphene on a protein model, HP35 by utilizing extensive molecular dynamics (MD) simulation methods. Our MD results elucidate that upon adsorption to the nanomaterial, HP35 undergoes a denaturation process initiated by the unraveling of the second helix of the protein and the loss of the proteins hydrophobic core. In detail, substantial alterations in various structural features of HP35 ensue, including alterations in hydrogen bonding, Q value, and RMSD. Subsequent analyses underscore that hydrophobic and van der Waals interactions (predominant), alongside electrostatic energy (subordinate), exert influence over the adsorption of HP35 on the fluorinated graphene surface. Mechanistic scrutiny attests that the unrestrained lateral mobility of HP35 on the fluorinated graphene nanomaterial primarily causes the exposure of HP35's hydrophobic core, resulting in the eventual structural denaturation of HP35. A trend in the features of 2D nanostructures is proposed that may facilitate the denaturation process. Our findings not only substantiate the potential toxicity of fluorinated graphene but also unveil the underlying molecular mechanism, which thereby holds significance for the prospective utilization of such nanomaterials in the field of biomedicine.