Laminated morphology of nontwisting β-sheet fibrils constructed via peptide self-assembly
Laminated morphology of nontwisting β-sheet fibrils constructed via peptide self-assembly
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DOI：
10.1021/ja054721f
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发表时间：
2005-11-30
影响因子：
15
通讯作者：
Pochan, DJ
中科院分区：
文献类型：
--
作者：
Lamm, MS;Rajagopal, K;Pochan, DJ
一种合成肽已经被从头设计出来，它可以自组装成呈现非扭曲、堆积形态的β-折叠纤维。堆叠形态由2.5 nm宽的细丝构成，这些细丝横向结合形成宽度超过50 nm、长度超过微米的扁平原纤层压板。每个原纤维的高度被限制在延伸的β-链构象中恰好一个肽单体的长度，大约7 nm。一旦组装，这些高度有序的二维结构在广泛的pH和温度范围内都是稳定的，并表现出类似于淀粉样纤维的特征。此外，可以通过pH和温度的动力学参数来控制聚集率和原纤层合度。最后，在多肽序列中两条形成β-片状结构的链之间存在的二脯氨酸多肽被证明是促进无扭曲的层状纤维形态的一个重要因素。
A synthetic peptide has been de novo designed that self-assembles into beta-sheet fibrils exhibiting a nontwisted, stacked morphology. The stacked morphology is constituted by 2.5 nm wide filaments that laterally associate to form flat fibril laminates exceeding 50 nm in width and micrometers in length. The height of each fibril is limited to the length of exactly one peptide monomer in an extended beta-strand conformation, approximately 7 nm. Once assembled, these highly ordered, 2-D structures are stable over a wide range of pH and temperature and exhibit characteristics similar to those of amyloid fibrils. Furthermore, the rate of assembly and degree of fibril lamination can be controlled with kinetic parameters of pH and temperature. Finally, the presence of a diproline peptide between two beta-sheet-forming strands in the peptide sequence is demonstrated to be an important factor in promoting the nontwisting, laminated fibril morphology.