Type I Collagen from Jellyfish Catostylus mosaicus for Biomaterial Applications
| Autor: | Frederik Fleissner, Sabine Pütz, Sachin Kumar, Sapun H. Parekh, Tobias Weidner, Yujen Wang, Zahra Rastian |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Jellyfish Protein subunit Biomedical Engineering 02 engineering and technology marine collagen Fibril Biomaterials 03 medical and health sciences biology.animal collagen molecular structure biology Chemistry Atomic force microscopy rat tail tendon collagen Biomaterial jellyfish 021001 nanoscience & nanotechnology biology.organism_classification type I collagen collagen biomaterials 030104 developmental biology Catostylus Biophysics 0210 nano-technology Alpha chain Type I collagen |
| Zdroj: | Rastian, Z, Pütz, S, Wang, Y J, Kumar, S, Fleissner, F, Weidner, T & Parekh, S H 2018, ' Type I Collagen from Jellyfish Catostylus mosaicus for Biomaterial Applications ', ACS Biomaterials Science and Engineering, vol. 4, no. 6, pp. 2115-2125 . https://doi.org/10.1021/acsbiomaterials.7b00979 |
| DOI: | 10.1021/acsbiomaterials.7b00979 |
| Popis: | Collagen is the predominant protein in animal connective tissues and is widely used in tissue regeneration and other industrial applications. Marine organisms have gained interest as alternative, nonmammalian collagen sources for biomaterial applications because of potential medical and economic advantages. In this work, we present physicochemical and biofunctionality studies of acid solubilized collagen (ASC) from jellyfish Catostylus mosaicus (JASC), harvested from the Persian Gulf, compared with ASC from rat tail tendon (RASC), the industry-standard collagen used for biomedical research. From the protein subunit (alpha chain) pattern of JASC, we identified it as a type I collagen, and extensive molecular spectroscopic analyses showed similar triple helical molecular signatures for JASC and RASC. Atomic force microscopy of fibrillized JASC showed clear fibril reassembly upon pH neutralization though with different temperature and concentration dependence compared with RASC. Molecular (natively folded, nonfibrillized) JASC was shown to functionalize rigid substrates and promote MC3T3 preosteoblast cell attachment and proliferation better than RASC over 6 days. On blended collagen-agarose scaffolds, both RASC and JASC fibrils supported cell attachment and proliferation, and scaffolds with RASC fibrils showed more cell growth after 6 days compared with those scaffolds with JASC fibrils. These results demonstrate the potential for this new type I collagen as a possible alternative to mammalian type I collagen for biomaterial applications. |
| Databáze: | OpenAIRE |
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