A novel method for analysis of the electrostatic complementarity of protein-protein interaction based on fragment molecular orbital method

[Display omitted] •A method for visualizing the electrostatic complementarity of PPI was developed.•Partial electron density and electrostatic potential were introduced.•Importance of induced electrostatic complementarity could be revealed. Here, the development of a method for analyzing the electro...

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Bibliographic Details
Published in:Chemical physics letters 2020-12, Vol.761, p.138103, Article 138103
Main Author: Ishikawa, Takeshi
Format: Article
Language:English
Subjects:
Electron density
Electrostatic potential
Fragment molecular orbital method
Protein-protein interaction
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Summary:[Display omitted] •A method for visualizing the electrostatic complementarity of PPI was developed.•Partial electron density and electrostatic potential were introduced.•Importance of induced electrostatic complementarity could be revealed. Here, the development of a method for analyzing the electrostatic complementarity of protein-protein interactions (PPIs) using fully quantum mechanical electron density (EDN) and electrostatic potential (ESP) is described. Partial EDN (pEDN) and ESP (pESP) of each protein were newly defined based on the fragment molecular orbital method. Illustrative calculations were performed for programmed cell death-1 (PD-1) and its ligand (PD-L1), which showed that the electrostatic complementarity of PD-1 and PD-L1 was clearly represented by the pEDN and pESP. Further analysis revealed that electrostatic complementarity induced by complex formation is important for binding between the proteins.
ISSN:0009-2614
1873-4448
DOI:10.1016/j.cplett.2020.138103