MPBuild: An Automated Pipeline for High-Fidelity Membrane Protein Simulation System Construction
Membrane proteins serve as the targets for 50% of FDA-approved drugs, but their dynamic characterization via molecular dynamics simulation is hindered by labor-intensive system preparation. To address this challenge, we developed MPBuild─an automated pipeline integrating structural repair, noncanonical component parametrization, and system assembly. Key innovations include (i) template-guided restoration of wild-type sequences and missing domains, (ii) automated force field generation for complex ligands, and (iii) decomposed PDB outputs enabling minute-scale system rebuilding. Benchmarked across 11 diverse membrane protein systems, MPBuild achieved processing times comparable to those of CHARMM-GUI when structural repair durations were excluded. Case studies validated the biophysical accuracy: Reproduced binding interfaces of GPR68-G<sub>q</sub>; accurately captured SSTR2/5 and octreotide interactions, and suggested potential novel motifs that may underlie receptor subtype selectivity. In summary, MPBuild serves as a powerful tool for high-throughput membrane protein drug discovery, offering an end-to-end solution that streamlines the entire process from system preparation to simulation.
Authors
- Changlin Tian (ORCID: https://orcid.org/0000-0001-9315-900X)
- Shenglong Ling (ORCID: https://orcid.org/0000-0002-8599-6219)
- Qing Liu (ORCID: https://orcid.org/0000-0002-0773-3843)
- Wei Ding
- Xiaojun Yao (ORCID: https://orcid.org/0000-0001-9958-8438)
Institutions
- Macau University of Science and Technology (MO)
- University of Science and Technology of China (CN)
- Shanghai Jiao Tong University (CN)
- Faculty (United Kingdom) (GB)
- Shanghai Advanced Research Institute (CN)
- Drug Discovery Laboratory (Norway) (NO)
- Institute for Advanced Study (DE)
- Beijing Academy of Science and Technology (CN)
- Macao Polytechnic University (MO)
Publication Details
- Journal
- Journal of Chemical Theory and Computation
- Published
- 2025-10-23
- DOI
- https://doi.org/10.1021/acs.jctc.5c01078
- Primary Topic
- Protein Structure and Dynamics
- Type
- article
- Field-Weighted Citation Impact
- 0.00