Rastian Zahra, Pütz Sabine, Wang YuJen, Kumar Sachin, Fleissner Frederik, Weidner Tobias, Parekh Sapun H
Department of Molecular Spectroscopy, Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.
The Persian Gulf Marine Biotechnology Research Center, The Persian Gulf Biomedical Sciences Research Institute, Bushehr University of Medical Sciences, Moallem St., 7514633341 Bushehr, Iran.
ACS Biomater Sci Eng. 2018 Jun 11;4(6):2115-2125. doi: 10.1021/acsbiomaterials.7b00979. Epub 2018 May 9.
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 (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.
胶原蛋白是动物结缔组织中的主要蛋白质，广泛应用于组织再生和其他工业领域。由于具有潜在的医学和经济优势，海洋生物作为生物材料应用的非哺乳动物胶原蛋白替代来源受到了关注。在这项工作中，我们对从波斯湾采集的水母酸性可溶胶原蛋白（JASC）进行了物理化学和生物功能研究，并与大鼠尾腱酸性可溶胶原蛋白（RASC，生物医学研究中使用的行业标准胶原蛋白）进行了比较。从JASC的蛋白质亚基（α链）模式来看，我们将其鉴定为I型胶原蛋白，广泛的分子光谱分析表明JASC和RASC具有相似的三螺旋分子特征。原子力显微镜对原纤维化的JASC进行观察，结果显示在pH值中和后，原纤维会明显重新组装，不过与RASC相比，其对温度和浓度的依赖性有所不同。研究表明，分子态（天然折叠、未原纤维化）的JASC能够使刚性底物功能化，并且在6天内比RASC更能促进MC3T3前成骨细胞的附着和增殖。在胶原蛋白 - 琼脂糖混合支架上，RASC和JASC原纤维均能支持细胞附着和增殖，与含有JASC原纤维的支架相比，含有RASC原纤维的支架在6天后显示出更多的细胞生长。这些结果表明，这种新型I型胶原蛋白在生物材料应用中作为哺乳动物I型胶原蛋白的潜在替代品具有可能性。
