Residue‑resolved dynamically averaged interaction analysis of direct factor Xa inhibitors by MD‑FMO combination calculations
Ryohei Yoshine, Yoshinori Hirano, Hideo Doi, Shun Kitahara, Kazuki Akisawa, Koji Okuwaki, Eiji Yamamoto, Kenji Yasuoka, Yuji Mochizuki · 2026
Read Residue‑resolved dynamically averaged interaction analysis of direct factor Xa inhibitors by MD‑FMO combination calculations by Ryohei Yoshine, Yoshinori Hirano, Hideo Doi, Shun Kitahara, Kazuki Akisawa, Koji Okuwaki, Eiji Yamamoto, Kenji Yasuoka, Yuji Mochizuki (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13221427.txt.
Description
Ryohei Yoshine and colleagues map, residue by residue, how four blood-thinning drugs grip their target enzyme, in a 2026 computational study. Edoxaban, betrixaban, apixaban, and rivaroxaban all block factor Xa, a key clotting enzyme. The team combined molecular dynamics simulations with fragment orbital calculations to average interactions over moving structures.
Six amino acid residues emerged as major contact points shared across all four drugs. Stabilization came from a mix of electrostatic, charge-transfer, and dispersion forces. The authors also tested how charged states changed binding for two of the drugs. A residue-level map like this can guide design of future anticoagulants with cleaner profiles.
Catalog record
| CREATOR | Ryohei Yoshine, Yoshinori Hirano, Hideo Doi, Shun Kitahara, Kazuki Akisawa, Koji Okuwaki, Eiji Yamamoto, Kenji Yasuoka, Yuji Mochizuki |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 28 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |