Abstract
Collagen has become a key-molecule in cell culture studies and in the tissue engineering field. Industrially, the principal sources of collagen are calf skin and bones which, however, could be associated to risks of serious disease transmission. In fact, collagen derived from alternative and riskless sources is required, and marine organisms are among the safest and recently exploited ones. Sea urchins possess a circular area of soft tissue surrounding the mouth, the peristomial membrane (PM), mainly composed by mammalian-like collagen. The PM of the edible sea urchin Paracentrotus lividus therefore represents a potential unexploited collagen source, easily obtainable as a food industry waste product. Our results demonstrate that it is possible to extract native collagen fibrils from the PM and produce suitable substrates for in vitro system. The obtained matrices appear as a homogeneous fibrillar network (mean fibril diameter 30–400 nm and mesh < 2 μm) and display remarkable mechanical properties in term of stiffness (146 ± 48 MPa) and viscosity (60.98 ± 52.07 GPa·s). In vitro tests with horse pbMSC show a good biocompatibility in terms of overall cell growth. The obtained results indicate that the sea urchin P. lividus can be a valuable low-cost collagen source for mechanically resistant biomedical devices.
Highlights
Collagen is the main structural component of animal tissues and shows peculiar mechanical properties conferring strength and elasticity to the tissue itself
The method we developed here leads to the extraction of intact collagen fibrils from P. lividus peristomial membrane (PM)
Besides the basic collagen matrix, the PM contains other different components, which represent a serious obstacle in obtaining a clean fibril suspension (Figure 2a)
Summary
Collagen is the main structural component of animal tissues and shows peculiar mechanical properties conferring strength and elasticity to the tissue itself. In tissue engineering the assembling of collagen fibrillar matrices usually includes fibrillization steps on partly defibrillated or hydrolized collagen [21,22] This method causes the production of fibrils which are only partially similar to the native ones in terms of structure and mechanical properties [22]. The present work is addressed to evaluate sea urchin collagen as a potential low-cost alternative for the production of scaffolds for biomedical applications This was achieved following different steps and approaches, including the development of a specific protocol for fibrillar collagen extraction and matrix preparation as well as a deep evaluation of the produced matrices in terms of ultrastructure, mechanical properties (stiffness and viscosity) and in vitro biocompatibility
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