In summary, two novel amphiphilic peptides, namely Ac-LIVKHH-NH 2 (P1) and Fmoc-LIVKHH-NH 2 (P2), were designed, with the aim to bind to metals. Hereby, the incorporation of histidine residues facilitates the binding to Zn(II) ions. Zn(II) ions at physiological conditions are able to bind to deprotonated imidazole moieties via metal-peptide crosslinking. Thus, these peptides, demonstrated their binding affinity to Zn(II) ions with the adjacent histidine residues at pH ~ 7, and led to formation of metallo-hydrogels via coordination polymerization. The addition of Zn(II) resulted in rapid gelation, as observed due to the responsiveness of these hydrogels to chemical stimuli, such as pH change. Structural analyses, including circular dichroism spectroscopy, scanning electron microscopy, and transmission electron microscopy, provided valuable information about the supramolecular architecture and micro-/nanostructure of the hydrogels. The morphology of their micro-and nanostructure revealed a flexible fibrous network influenced with observable changes in the presences of Zn(II). Furthermore, at increasing peptide concentrations, while Zn(II) ions do not significantly impact the secondary conformation, they exhibit a stabilizing effect on the structure. Rheological characterization demonstrated the viscoelastic properties of the peptide hydrogels, along with their mechanical stiffness and thixotropic behavior. The incorporation of Zn(II) ions significantly enhanced the mechanical strength (and storage modulus) especially at physiological conditions. P2 hydrogels showed thixotropic behavior in presence and absence of Zn(II) with rapid self-healing ability upon removal of shear force. To the best of our knowledge, the mechanical strength reported for our peptides, outperformed any other known (metallo)-hydrogels based on short peptides. As such, findings pave the way for the development of novel biomaterials with tailored properties for biomedical applications, including drug delivery, tissue engineering and wound healing/ management. Further, the thixotropic behavior of these peptides makes them ideal candidates for 3D printing or as injectable biomaterials for therapy.