Tuning the gelation behavior of short laminin derived peptides via solvent mediated self-assembly

Controlling the self-assembly pathways through solvent mediated approach can be an effective means to create complex, multifunctional structures. However, predicting the effect of solvent environment on both solubility of the monomer and their self-assembling behaviour remains a challenge. Our work mainly aims to understand the role of solvents in driving the supramolecular self-assembly of structurally related bioinspired pentapeptides (IKVAV and YIGSR), derived from native laminin protein. The exploration of the short sequences from this useful functional protein is still in its infancy. An N-terminal hydrophobic modification of IKVAV and YIGSR has been used to illustrate the gelator-gelator and gelator-solvent intermolecular interactions. Microscopic investigation of hydrophobic derivatives showed the transformation of fibrous morphology to sheet like structures, on varying solvent polarity from aqueous-organic mixture to aqueous solvent. Interestingly, these gels possess mechano-responsive and thermo-reversible properties, which also showed the remarkable solvent susceptibility. Our study clearly indicates that judicious choice of solvents may help in designing new soft materials with controlled properties, lesser defects and higher reproducibility.