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Ligand field molecular dynamics simulation of Pt(II)-phenanthroline binding to N-terminal fragment of amyloid-β peptide
by
Turner, Matthew
, Platts, James A
, Deeth, Robert J
, Mutter, Shaun T
in
Algorithms
/ Binding
/ Biology and Life Sciences
/ Bonding
/ Chemical bonds
/ Chemistry
/ Gyration
/ Hydrogen
/ Hydrogen bonding
/ Ligands
/ Mechanics
/ Medicine and Health Sciences
/ Metals
/ Molecular dynamics
/ Peptides
/ Physical Sciences
/ Platinum
/ Proteins
/ Residues
/ Salts
/ Simulation
/ Variation
/ β-Amyloid
2018
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Ligand field molecular dynamics simulation of Pt(II)-phenanthroline binding to N-terminal fragment of amyloid-β peptide
by
Turner, Matthew
, Platts, James A
, Deeth, Robert J
, Mutter, Shaun T
in
Algorithms
/ Binding
/ Biology and Life Sciences
/ Bonding
/ Chemical bonds
/ Chemistry
/ Gyration
/ Hydrogen
/ Hydrogen bonding
/ Ligands
/ Mechanics
/ Medicine and Health Sciences
/ Metals
/ Molecular dynamics
/ Peptides
/ Physical Sciences
/ Platinum
/ Proteins
/ Residues
/ Salts
/ Simulation
/ Variation
/ β-Amyloid
2018
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Ligand field molecular dynamics simulation of Pt(II)-phenanthroline binding to N-terminal fragment of amyloid-β peptide
by
Turner, Matthew
, Platts, James A
, Deeth, Robert J
, Mutter, Shaun T
in
Algorithms
/ Binding
/ Biology and Life Sciences
/ Bonding
/ Chemical bonds
/ Chemistry
/ Gyration
/ Hydrogen
/ Hydrogen bonding
/ Ligands
/ Mechanics
/ Medicine and Health Sciences
/ Metals
/ Molecular dynamics
/ Peptides
/ Physical Sciences
/ Platinum
/ Proteins
/ Residues
/ Salts
/ Simulation
/ Variation
/ β-Amyloid
2018
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Ligand field molecular dynamics simulation of Pt(II)-phenanthroline binding to N-terminal fragment of amyloid-β peptide
Journal Article
Ligand field molecular dynamics simulation of Pt(II)-phenanthroline binding to N-terminal fragment of amyloid-β peptide
2018
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Overview
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.
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