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Researchers from the National Nanoscience Center have used STM technology to study the assembly and regulation of peptides at the single molecule level, and have published a series of work. In 2011, they used STM to confirm the core fragments and folding sites of amyloid peptide assembly and aggregation, providing a novel analytical method for studying the assembly structure of non-crystalline proteins (Proc. Natl. Acad. Sci. USA, 2011 , 108, 19605, etc.), but due to the diversity of the conformation of the polypeptide on the surface and the difference in adsorption stability, the use of STM to identify the amino acid sequence in the polypeptide is still very challenging.
In this study, the researchers used STM combined with molecular dynamics simulations to study the effect of amino acid residue sequences on the stability of the adsorption conformation of the block model polypeptide on the solid surface, and found that the contrast difference between the STM image and the model polypeptide The sequences are related, and molecular dynamics simulations have found that the differences in binding energy and contrast of different amino acid residues on the graphite surface are also consistent, indicating the influence of the peptide sequence on the assembly conformation and assembly characteristics, suggesting the use of STM for peptide The possibility of sequence identification. This study is helpful for understanding the influence of side group structure and sequence on the assembly process, assembly driving force and assembly structure during the assembly process of peptides.
This work was supported by the Ministry of Science and Technology's major research plan and the Fund's major research plan.
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