LAUSR

Non-covalent interactions among short peptides and proteins led to their molecular self-assembly into supramolecular packaging, which provides the fundamental basis of life. These biomolecular assemblies are highly susceptible to the environmental conditions, including temperature, light, pH, and ionic concentration, thus inspiring the fabrication of a new class of stimuli-responsive biomaterials. Here, we report for the first time the cooperative effect of the divalent metal ions to promote hydrogelation in the short collagen inspired self-assembling peptide for developing advanced biomaterials. Introduction of the biologically relevant metal ions (Ca2+ /Mg2+ ) to the peptide surpasses its limitation to self-assemble into a multi-scale structure at physiological pH. In particular, in presence of metal ions, the negatively charged peptide showed a distinct shift in its equilibrium point of gelation and demonstrated conversion from sol to gel and thus enabling the scope of fabricating an advanced biomaterial for controlling cellular behaviour. Interestingly, tunable mechanical strength and improved cellular response were observed within ion-coordinated peptide hydrogels compared to the peptide gelator. Microscopic analyses, rheological assessment, and biological studies established the importance of utilizing a novel strategy by simply using metal ions to modulate the physical and biological attributes of CIPs to construct next-generation biomaterials. This article is protected by copyright. All rights reserved.