This study explored the role of fibrinogen hydrolyzed peptides in enhancing myosin thermal gelation properties. We investigated the impact of disrupted hydrophobic interactions and disulfide bonds on the characteristics of myosin-fibrinogen peptide composite gels using sodium dodecyl sulfate (SDS) and dithiothreitol (DTT). Disrupted hydrophobic interactions led to decreased gel texture, water-holding capacity, rheological properties and irregular pore distribution, emphasizing their critical role in gel integrity. The reduction of disulfide bonds during gelation resulted in enhanced water loss during cooking and the formation of larger, more open gel pores. Molecular docking and dynamic simulations of Pep1 revealed strong binding to myosin through hydrophobic interactions, hydrogen bonds and van der Waals forces, promoting conformational changes and partial myosin unfolding, which further supported the molecular interactions driving gelation. These findings provided valuable insights into how fibrinogen-derived peptides influenced myosin gelation, presenting potential for developing advanced gel systems in food applications.