The proposed Force-guided Bridge Matching (FBM) model has significant potential applications beyond peptide systems, particularly in the study of larger biomolecules and materials science. In the realm of biomolecular research, FBM can be utilized to simulate the dynamics of complex proteins, nucleic acids, and protein-ligand interactions. The model's ability to incorporate physics priors, such as energy and force fields, allows for more accurate representations of the conformational landscapes of larger biomolecules, which are often characterized by intricate folding patterns and multiple metastable states. This capability can enhance our understanding of protein folding mechanisms, allosteric regulation, and the binding affinities of drug candidates.
In materials science, FBM can be applied to study the dynamics of polymers, nanomaterials, and crystalline structures. The model's efficiency in time-coarsened dynamics can facilitate the exploration of phase transitions and material properties under various conditions, such as temperature and pressure changes. By accurately simulating the molecular interactions and dynamics of materials, FBM can contribute to the design of new materials with tailored properties, such as improved mechanical strength, thermal stability, or conductivity. Furthermore, the model's transferability to unseen systems can aid in the rapid screening of material candidates for specific applications, thereby accelerating the materials discovery process.