Abstract
Fibrillar collagen is the major protein in the extracellular matrix and regulates cell behavior via chemical and mechanical cues. The key structural element of collagen fibrils is the axially repeating D-period, formed by the lateral association of collagen triple helices. We have developed fibril-forming collagen mimetic peptides (FCMPs) with repeated amino acid sequences, which form fibrils having D-period-like structures. Containing over 100 amino acid residues, these peptides are produced by bacterial expression using designed genes. Here, we report the fibrillogenesis of a new FCMP containing an α-helix coiled coil domain. The latest findings highlight the importance of the amino acid sequence periodicity in FCMP fibril formation. Additionally, our results demonstrate the remarkable adaptability of collagen fibrils' molecular packing. Mirroring native collagen fibrils, in both the structure and the fibrillogenesis process, these FCMPs are useful molecular tools for advancing collagen research and developing novel biomaterials.
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