A Thermally Reformable Protein Polymer
A Thermally Reformable Protein Polymer
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DOI：
10.1016/j.chempr.2020.09.020
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发表时间：
2020-11-05
期刊：
影响因子：
23.5
通讯作者：
Fulton, David A.
中科院分区：
文献类型：
--
作者：
Dura, Gema;Peters, Daniel T.;Fulton, David A.
通过自组装蛋白质容易形成的复杂生物材料可以改变再生医学和3D细胞培养。然而，尽管通过短肽容易地实现，但是由具有确定的三级结构的蛋白质组装的材料仍然是罕见的。细菌菌毛蛋白，荚膜抗原片段1（Caf 1），形成通过动力学稳定的非共价相互作用连接的亚基的长聚合物，其可以进一步化学交联成各种水凝胶。我们在这里报告，Caf1聚合物或水凝胶完全热分解成单个亚基是完全可逆的，产量高。这个简单的功能赋予Caf1聚合物具有出色的合成和材料的可能性，并证明，我们描述了复杂的生物活性共聚物的体外组装，并提供可熔蛋白质水凝胶的应用实例。我们预计，这些多功能聚合蛋白质的高效和可逆组装将显着提高蛋白质生物材料的临床和工业应用的发展。
Complex biomaterials easily formed by self-assembling proteins could transform regenerative medicine and 3D cell culture. However, although readily achieved by short peptides, materials assembled from proteins with a defined tertiary structure are still rare, The bacterial fimbrial protein, capsular antigen fragment 1 (Caf1), forms long polymers of subunits linked by kinetically stable non-covalent interactions, which can be further chemically crosslinked into a variety of hydrogels. We report here that the complete thermal dissociation of Caf1 polymers or hydrogels into individual subunits is fully reversible with high yield. This simple feature endows the Caf1 polymer with outstanding synthetic and materials possibilities and, to demonstrate, we describe the in vitro assembly of complex bioactive copolymers and provide example applications of meltable protein hydrogels. We anticipate that the highly efficient and reversible assembly of these multifunctional polymeric proteins will enhance significantly the development of proteinaceous biomaterials for clinical and industrial applications.