Potency of anti-trematode in inhibiting cathepsin-2L and cathepsin-5L of Fasciola gigantica using homology, docking, and molecular dynamics
Henni Vanda, Farida Athaillah, Wahyu Eka Sari, Frengki Frengki, Nurliana Nurliana, Muhammad Hambal · 2024
Read Potency of anti-trematode in inhibiting cathepsin-2L and cathepsin-5L of Fasciola gigantica using homology, docking, and molecular dynamics by Henni Vanda, Farida Athaillah, Wahyu Eka Sari, Frengki Frengki, Nurliana Nurliana, Muhammad Hambal (2024) 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-11682782.txt.
Description
Henni Vanda, Farida Athaillah, Wahyu Eka Sari, Frengki Frengki, Nurliana Nurliana, and Muhammad Hambal screen fluke drugs in computer models in a 2024 paper. The target is a tropical liver fluke, Fasciola gigantica. Its cathepsin enzymes help it feed and evade immunity. Blocking them could power new anti-fluke drugs.
Six commercial dewormers were docked against two cathepsins. All six bound both enzymes in the simulations. Clorsulon bound the first enzyme most tightly of the set. Closantel led the pack against the second enzyme. Motion simulations showed both pairings stay stable over time. Old drugs may be repurposed against these targets. Lab tests are the next step they propose.
Catalog record
| CREATOR | Henni Vanda, Farida Athaillah, Wahyu Eka Sari, Frengki Frengki, Nurliana Nurliana, Muhammad Hambal |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 21 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |