Molecular self-assembly refers to the spontaneous and reversible organization of molecules into higher-order structures. This phenomenon is highly prevalent in nature, where assembled entities such as DNA or proteins exhibit distinctive biological functions. Peptide-based supramolecular architectures stand out for their biocompatibility, biodegradability, and ease of synthesis. Such structures are based on the organization of peptides into secondary structures such as βsheet or α-helix, which can then undergo hierarchical and multiscale assembly processes. These structures rely on noncovalent interactions, such as hydrogen bonds, hydrophobic interactions, van der Waals forces, electrostatic-and π-π interactions, respectively. In aqueous solution, these self-assembled peptide architectures can also yield hydrogels by entrapping large amounts of water. To generate peptide hydrogels, the use of short peptides is particularly appealing as it offers robustness, scalability, and cost-effectiveness. Besides the rational design of short peptides, a common strategy to modulate the self-assembling properties involves protection of the N-and/or C-terminus through use of acetyl or large aromatic groups such as fluorenylmethoxycarbonyl protecting group (Fmoc). This modification reduces charge repulsions and introduces π-stacking/hydrophobic contributions, thereby promoting self-assembly and hydrogel formation. Metal ions are frequently employed to trigger peptide assembly, thereby leading to hydrogelation. Such metal ioncoordinated peptide hydrogels hold significant potential, as they exploit the unique physicochemical characteristics of metals, such as Zn(II), which play essential roles in biological processes and disease-related protein assemblies. For instance, zinc, known for its antimicrobial and bacteriostatic properties, is beneficial in wound healing and infection prevention applications. Additionally, zinc plays a crucial role in collagen synthesis, imparting tensile strength to the newly formed tissue at the wound site. However, a comprehensive understanding of the impact of metal coordination on peptide assembly processes affording hydrogels remains limited. The addition of metal ions through metal-ligand coordination offers a method to tune the mechanical stiffness of hydrogels, complementing the other approaches of manipulating crosslink density, peptide concentration, or pH, which can influence the essential biological functions of such gels. Metal salts or complexes have been utilized to induce gelation in peptide solutions, enabling formation of stable gels through ordered aggregates formed by metal-peptide interactions. For example, Mishra and coworkers investigated the influence of metal salts on the self-assembling behavior of Ac-LIVAGD and Ac-IVD, revealing how cation coordination and ionic strength affect hydrogelation, facilitating controlled modulation of the mechanical properties of Ac-LIVAGD hydrogel for targeted biomedical applications. Herein, short amphiphilic peptides were developed with specific binding affinity for biologically benign metal salts, particularly zinc. In aqueous conditions, the interactions between the histidine moieties of peptides and Zn(II) resulted in the formation of a coordination polymer incorporating zinc as a crosslinker, ultimately leading to metallo-hydrogel formation. We investigated the impact of N-terminus modifications on hydrogel formation, whereby Fmoc-protected peptides were found to yield stiffer hydrogels due to favorable π-π stacking effects. This comprehensive analysis demonstrates the zinc-responsive behavior of the metallo-hydrogels, covering variations in zinc content ranging from 0 to 0.5 equivalents. The influence of Zn(II) on their mechanical properties, viscoelastic character, and recovery capabilities was also assessed. The observed effects demonstrate how zinc plays a key role in enhancing the overall performance of the metallo-hydrogels, providing valuable insights into their potential applications in the field of materials science and biomaterials.