Template-directed assembly of a de novo designed protein
Template-directed assembly of a de novo designed protein
复制标题
DOI：
10.1021/ja0261271
复制
发表时间：
2002-06-19
影响因子：
15
通讯作者：
Hecht, MH
中科院分区：
文献类型：
--
作者：
Brown, CL;Aksay, IA;Hecht, MH
许多天然存在的生物材料都是由β折叠蛋白层和无机矿物层交替排列而成的层状结构，这些有序的层状结构通常具有与非生物材料显著不同的结构和力学性能。构建新型生物材料的一个重要步骤是创造复合材料，其中新设计的蛋白质组装成有序结构。为了实现这一目标，我们在高度有序的热解石墨（HOPG）表面上分层了ade novoprotein。该蛋白衍生自设计成折叠成两亲性β折叠结构的新序列的组合文库。原子力显微镜显示，蛋白质在HOPG表面组装成有序的纤维，在三个方向上以120°彼此对齐。有序区域的对称性和范围表明，石墨表面下的六边形晶格模板数百万蛋白质分子组装成一个高度有序的结构。
Many naturally occurring biomaterials are composed of laminated structures in which layers of β-sheet proteins alternate with layers of inorganic mineral. These ordered laminates often have structural and mechanical properties that differ significantly from those of nonbiological materials. An important step in the construction of novel biomaterials is the creation of composites wherein ade novodesigned protein assembles into an ordered structure. To achieve this goal, we layered ade novoprotein onto the surface of highly ordered pyrolytic graphite (HOPG). The protein was derived from a combinatorial library of novel sequences designed to fold into amphiphilic β-sheet structures. Atomic force microscopy reveals that the protein assembles on the HOPG surface into ordered fibers aligned in three orientations at 120° to each other. The symmetry and extent of the ordered regions indicate that the hexagonal lattice underlying the graphite surface templates assembly of millions of protein molecules into a highly ordered structure.