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首页> 外文期刊>Biomaterials >Some properties of keratin biomaterials: kerateines.
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Some properties of keratin biomaterials: kerateines.

机译：角蛋白生物材料的一些特性：角蛋白。

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摘要

Keratins are a family of structural proteins that can be isolated from a variety of tissues. "Soft" keratins are cytoskeletal elements found in epithelial tissues while protective tissues such as nails, hooves, and hair are composed of "hard" keratins. Hard keratins have been the subject of biomaterials investigations for more than three decades. Numerous methods exist for denaturing these proteins which are characterized by a high sulfur content and extensive disulfide bonding, under either oxidative or reductive conditions, extracting them from tissue and processing them into various physical states such as gels, films, coatings, and fibers. Kerateines or keratoses (oxidatively or reductively derived, respectively), alone or in combination with other biomaterials, have been tested in a small number of systems to demonstrate feasibility for medical applications such as wound healing, bone regeneration, hemostasis, and peripheral nerve repair. These investigations have shown generally good compatibility with cells and tissues, but the focus of prior investigations has been fairly narrow, and as a result there is relatively little published data on the general behavior of keratin biomaterials in biological systems beyond cell culture assays. The goal of this study was to produce a reduced form of keratin biomaterial, kerateine, using a typical and well-published technique, and characterize several aspects of its behavior that may have implications to its general use as a biomaterial. Kerateines were extracted from human hair, fabricated into gels and porous scaffolds, characterized, and placed into biological systems to determine their interactions with cells and tissue. Initially, the proteins were analyzed for molecular weight and amino acid content, as well as their ability to facilitate cell adhesion and proliferation. Crosslinked hydrogels were investigated for their hydrolytic stability in vitro; the micro-architecture and in vivo tissue response of lyophilized gels was also studied. These experiments both confirmed and expanded earlier findings that kerateines demonstrate excellent compatibility in biological systems.
机译：角蛋白是可以从多种组织中分离的结构蛋白家族。 “软”角蛋白是在上皮组织中发现的细胞骨架元素，而保护性组织（如指甲，蹄和头发）则由“硬”角蛋白组成。超过三十年以来，硬角蛋白一直是生物材料研究的主题。存在多种方法来使这些蛋白质变性，这些蛋白质的特征在于在氧化或还原条件下具有高硫含量和广泛的二硫键，将其从组织中提取出来并将其加工成各种物理状态，例如凝胶，薄膜，涂层和纤维。已在少数系统中对单独或与其他生物材料组合的丁二胺酮或角蛋白聚糖（分别氧化或还原衍生）进行了测试，以证明其在医学应用中的可行性，例如伤口愈合，骨再生，止血和周围神经修复。这些研究已经显示出与细胞和组织的良好相容性，但是先前研究的重点一直很狭窄，因此，除了细胞培养测定法以外，关于角蛋白生物材料在生物系统中的一般行为的公开数据还很少。这项研究的目的是使用一种典型且广为人知的技术生产一种减少形式的角蛋白生物材料角蛋白，并表征其行为的几个方面，这些方面可能会影响其作为生物材料的普遍用途。从人的头发中提取氯丁胺盐，制成凝胶和多孔支架，进行表征，然后将其置于生物系统中以确定它们与细胞和组织的相互作用。最初，分析蛋白质的分子量和氨基酸含量，以及它们促进细胞黏附和增殖的能力。研究了交联水凝胶的体外水解稳定性。还研究了冻干凝胶的微结构和体内组织反应。这些实验都证实并扩展了早期发现，即角蛋白在生物系统中具有优异的相容性。

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