Abstract
This study was conducted to implement fish collagen hydrolysate as a substrate for synthesizing a nanophasic hydroxyapatite (HA) coating that would display superior osteoinductivity than HA derived from collagen (C/HA) and to comprehend the contribution of secondary structure on HA synthesis. Collagen type I was isolated from mullet skin and fragmented to obtain collagen hydrolysate (MCH). CD, FTIR, XRD, DLS and MS studies revealed that the MCH peptides oriented in polyproline-II conformation and coiled to form a mimic-helix with a packing distance of 0.885 nm. Multiple helices self-assembled into a quasi-fibrillar network with a diameter of 931 nm. The MCH was suspended in HA-nucleating solution to form MCH/HA nanocomposite crystals, which exhibited HA-specific planes in XRD with crystal orientation towards the quasi-fibrillar axis and a % crystallinity of 96.04. MCH/HA crystals were plate-shaped with an average size of 55.4 nm and a Ca/P ratio of 1.77 with moderate resilience (9.9 GPa) and high wettability. Consequently, osteoblasts cultured on MCH/HA coated-Ti surface proliferated faster and expressed 1.2–2 times higher levels of osteogenic differentiation markers when compared to C/HA-coated and uncoated surfaces. The study identified MCH/HA to be a superior coating material, by virtue of the unique quasi-fibrillar architecture of MCH.
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