ArticleJournal of molecular modeling2022
Homodimeric complexes of the 90-231 human prion: a multilayered computational study based on FMO/GRID-DRY approach.
Article in Journal of molecular modeling, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 9 citations in OpenAlex.
- Combining the Fragment Molecular Orbital and GRID Approaches for the Prediction of Ligand-Metalloenzyme Binding Affinity: The Case Study of hCA II Inhibitors.Molecules (Basel, Switzerland) · 2024Article
- A computational insight on the aromatic amino acids conjugation with [Cp*Rh(HJournal of molecular modeling · 2023Article
- Improving the accuracy of the FMO binding affinity prediction of ligand-receptor complexes containing metals.Journal of computer-aided molecular design · 2023Article
- Structural Reshaping of the Zinc-Finger Domain of the SARS-CoV-2 nsp13 Protein Using Bismuth(III) Ions: A Multilevel Computational Study.Inorganic chemistry · 2022Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
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Abstract
The molecular interaction properties and aggregation capabilities disclosed by PrP-E200K, a pathogenic mutant of the human prion protein, were investigated in detail using multilayered computational approaches. In a previous work, we reported that the electrostatic complementarity between region1 (negative) and region3 (positive) has been assumed to lead to a head-to tail interaction between 120 and 231 PrP-E200K units and to initiation of the aggregation process. In this work, we extended the PrP-E200K structure by including the unstructured 90-120 segment which was found to assume different conformations. Plausible models of 90-231 PrP-E200K dimers were calculated and analyzed in depth to identify the nature of the involved protein-protein interactions. The unstructured 90-120 segment was found to extend the positively charged region3 involved in the association of PrP-E200K units which resulted to be driven by hydrophobic interactions. The combination of molecular dynamics, protein-protein docking, grid-based mapping, and fragment molecular orbital approaches allowed us to provide a plausible mechanism of the early state of 90-231 PrP-E200K aggregation, considered a preliminary step of amyloid conversion.
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