This study utilizes atomistic molecular dynamics simulations to demonstrate the structural resilience of Interleukin-4 (IL-4) in the absence of its native disulfide bonds (Cys3-Cys127 and Cys24-Cys65). Despite the loss of these key covalent linkages, IL-4 retained its overall four-helix bundle structure, demonstrating significant structural resilience. The disruption of the Cys3-Cys127 bond was compensated by the formation of stabilizing inter-terminal noncovalent interactions, whereas the removal of the Cys24-Cys65 bond led to increased flexibility in loop regions and the C-terminal domain. Additionally, grafting of charge-neutral Atom Transfer Radical Polymerization (ATRP) initiators onto surface lysine residues creates localized interaction hubs that act as secondary stabilizing scaffolds. These findings provide a framework for engineering robust, disulfide-independent cytokine scaffolds for biotherapeutic applications, supporting Sustainable Development Goals 3 and 9.