Planar Boronic Graphene and Nitrogenized Graphene Heterostructure for Protein Stretch and Confinement

• Published in: Biomolecules (Basel, Switzerland) Switzerland), 2021-11, Vol.11 (12), p.1756
• Main Authors: Su, Xuchang, He, Zhi, Meng, Lijun, Liang, Hong, Zhou, Ruhong
• Format: Article
• Language: English
• Subjects: alpha-Synuclein - chemistry; Amino acids; Amyloid beta-Peptides - chemistry; Animals; Atomic force microscopy; Boron; Boron - chemistry; boronic graphene; Graphene; Graphite - chemistry; Humans; inplane heterostructure; Intrinsically Disordered Proteins - chemistry; Models, Molecular; Molecular Dynamics Simulation; Nitrogen - chemistry; nitrogenized graphene; Peptide Fragments - chemistry; Peptides; Peptides - chemistry; Polyglutamine; Protein Conformation; protein stretch and confinement; Proteins; Simulation; Single Molecule Imaging; Synuclein; Trinucleotide repeat diseases; β-Amyloid
• ISSN: 2218-273X; 2218-273X
• DOI: 10.3390/biom11121756

Single-molecule techniques such as electron tunneling and atomic force microscopy have attracted growing interests in protein sequencing. For these methods, it is critical to refine and stabilize the protein sample to a "suitable mode" before applying a high-fidelity measurement. Here, we show that a planar heterostructure comprising boronic graphene (BC ) and nitrogenized graphene (C N) sandwiched stripe (BC /C N/BC ) is capable of the effective stretching and confinement of three types of intrinsically disordered proteins (IDPs), including amyloid-β (1-42), polyglutamine (Q42), and α-Synuclein (61-95). Our molecular dynamics simulations demonstrate that the protein molecules interact more strongly with the C N stripe than the BC one, which leads to their capture, elongation, and confinement along the center C N stripe of the heterostructure. The conformational fluctuations of IDPs are substantially reduced after being stretched. This design may serve as a platform for single-molecule protein analysis with reduced thermal noise.