Ensemble Molecular Dynamics of a Protein-Ligand Complex: Residual Inhibitor Entropy Enhances Drug Potency in Butyrylcholinesterase.

Butyrylcholinesterase is a key enzyme that catalyzes the hydrolysis of the neurotransmitter acetylcholine and shows an increased activity in patients suffering from Alzheimer's disease (AD), making this enzyme a primary target in treating AD. Central to this problem, and to similar scenarios involving biomolecular recognition, is our understanding of the nature of the protein-ligand complex. The butyrylcholinesterase enzyme was studied via all-atom, explicit solvent, ensemble molecular dynamics simulations sans inhibitor and in the presence of three dialkyl phenyl phosphate inhibitors of known potency to a cumulative sampling of over 40 μs.

A meta-analysis of the fusion rate from surgical treatment for odontoid factures: anterior odontoid screw versus posterior C1-C2 arthrodesis.

Purpose: Surgical treatment for odontoid fractures is widely performed in practice. However, the choice of different surgical procedures remains controversial. Regardless of the surgical technique, the fusion situation is one of the important factors that affect the clinical efficacy.