Sacrificial bonding is a ubiquitous cross-linking strategy for increasing toughness that is found throughout nature in various biological materials such as bone, wood, silk and mussel byssal threads. However, the molecular mechanism of sacrificial bonding remains only poorly understood. Molecular modeling possesses a strong potential to provide insights into the behavior of these cross-links. Here we use Monte Carlo simulations to investigate the effect of reversible sacrificial binding sites on the mechanical properties of single linear polymer chains based on load-bearing metalloproteins found in the mussel byssus. It is shown that the topology of the bonds determines the position and spacing of sacrificial force peaks, while the height of these peaks is intimately tied to the magnitude of thermal fluctuations in the chain that are dependent on effective chain length. These results bear important implications for understanding natural systems and for the generation of strong and ductile biomimetic polymers.