There is an increasing demand for biocompatible materials in biomedical applications. Herein, we report a modified α-helical decapeptide segment from the cardiac troponin C, which self-assembles into fibers with a secondary β-sheet structure. These fibers cross-link via a novel supramolecular threading mechanism which results in an atypical stiff hydrogel (G′ ≈ 13 kPa). In this work, we provide a first insight into the understanding of such remarkable cross-linking mechanism, which will aid in the development of new biomaterials with unique properties
