2026-10-13T04:37:03Z https://api.figshare.com/v2/oai

oai:figshare.com:article/33803221 2026-09-15T15:33:41Z portal_1197 item_type_3 month_year_09_2026

Data for Ligand field molecular dynamics simulation of Pt(II)-phenanthroline binding to N-terminal fragment of amyloid-beta peptide James A. Platts (1440922) Matthew A. P. Turner (9177095) Shaun T. Mutter (2157253) Robert J. Deeth (1362144) Molecular dynamics -- Simulation methods Ligand field theory Amyloid beta-protein -- Research Migrated from ePrints We report microsecond timescale molecular dynamics simulation of the complex formed between Pt(II)-phenanthroline and the 16 N-terminal residues of the Aβ peptide that is implicated in the onset of Alzheimer’s disease, along with equivalent simulations of the metal-free peptide. Simulations from a variety of starting points reach equilibrium within 100 ns, as judged by root mean square deviation and radius of gyration. Platinum-bound peptides deviate rather more from starting points, and adopt structures with larger radius of gyration, than their metal-free counterparts. Residues bound directly to Pt show smaller fluctuation, but others actually move more in the Pt-bound peptide. Hydrogen bonding within the peptide is disrupted by binding of Pt, whereas the presence of salt-bridges are enhanced.<br><br>Data record consists of a data archive file in .tar.gz format. DL_POLY Classic input and output files for 10 MD simulations: 5 of free peptide, 5 with Pt(phen). 2017-11-17T00:00:00Z Dataset Dataset 10.82444/warw.33803221.v1 https://figshare.com/articles/dataset/Data_for_Ligand_field_molecular_dynamics_simulation_of_Pt_II_-phenanthroline_binding_to_N-terminal_fragment_of_amyloid-beta_peptide/33803221 CC BY 4.0