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N-terminal residues of α-synuclein, which is a crucial region for physiological function and neurodegeneration in Parkinson’s disease, have been of particular interest in the study of α-synuclein function and the development of novel therapeutic strategies against this illness. Although the biochemical and biophysical properties of the N-terminal region have been extensively investigated, its binding mechanism has yet to be revealed. In this paper, the simulation results of human α-synuclein (hαSN) N-terminus and its complex with different small biomolecules are presented using molecular dynamics (MD) simulations and explicit solvent electrostatic (ES) calculations. The binding model of the N-terminus of hαSN interacting with cytochrome c (hαSN-cyt c) and glycine (hαSN-gly) have been proposed on the basis of these results. The binding free energies and molecular interaction mechanisms between the N-terminus of hαSN and different small biomolecules are also discussed. The results show that the binding of the N-terminus of hαSN to small biomolecules is accompanied by a charge transfer. The stability of the complex is due to the formation of the hydrogen bonds between the N-terminus of hαSN and the small biomolecules and the hydrophobic interactions between hαSN and the small biomolecules. The findings provide a theoretical basis for elucidating the interaction of the N-terminus of hαSN with other biomolecules, as well as the design of novel drugs and nanomedicines.Small Size Abdominal Aortic Aneurysm (≤3 cm): Choice of Endovascular or Surgical Treatment.
To investigate the outcomes of small size abdominal aortic aneurysm (AAA) treated by endovascular stent-grafting or open surgical repair (OSR). A total of 195 patients with small-size AAA (\

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