Le-Dao, Hoang-Anh and Dinh, Thuan-Thien and Tran, Thuoc Linh and Lee, Vannajan Sanghiran and Tran-Van, Hieu (2024) Molecular dynamics simulations reveal novel interacting regions of human prion protein to Brucella abortus Hsp60 protein. Molecular Biotechnology, 66 (4, SI). pp. 687-695. ISSN 1073-6085, DOI https://doi.org/10.1007/s12033-023-00655-9.
Full text not available from this repository.Abstract
The distinctive morphology characteristics of microfold cells (M cells) allow the vaccine antigen not only to interact with immune cells directly, but also to effectively stimulate mucosal immune responses via receptors on its apical surface. Human prion protein, a transmembrane receptor for Brucella abortus Hsp60, is highly expressed on the M cell surface. Nonetheless, this protein tends to express in inclusion body in prokaryotic hosts. In this study, the shorter interacting regions of human prion protein were identified via computational methods such as docking and molecular dynamics simulations to minimize its aggregation tendency. The computational calculations revealed three novel human prion protein-interacting regions, namely PrP125, PrP174, and PrP180. In accordance with in silico prediction, the biologically synthesized peptides fusing with GST tag demonstrated their specific binding to Hsp60 protein via pull-down assay. Hence, this finding laid the groundwork for M-cell targeting candidate validation through these newly identified interacting regions.
| Item Type: | Article |
|---|---|
| Funders: | UNSPECIFIED |
| Uncontrolled Keywords: | Hsp60 protein; Homology modeling; Human prion protein; M cell; Molecular docking; Molecular dynamics (MDs); Pull-down assay |
| Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology T Technology > T Technology (General) |
| Divisions: | Faculty of Science > Department of Chemistry |
| Depositing User: | Ms. Juhaida Abd Rahim |
| Date Deposited: | 15 Aug 2024 07:48 |
| Last Modified: | 15 Aug 2024 07:48 |
| URI: | http://eprints.um.edu.my/id/eprint/46077 |
Actions (login required)
 |
View Item |
