Self-assembly of Aβ(10-35)-PEG block copolymer fibrils
Self-assembly of Aβ(10-35)-PEG block copolymer fibrils
复制标题
DOI：
10.1021/ja991233x
复制
发表时间：
1999-08-18
影响因子：
15
通讯作者：
Thiyagarajan, P
中科院分区：
文献类型：
--
作者：
Burkoth, TS;Benzinger, TLS;Thiyagarajan, P
{β}-折叠二级结构在能量上不仅依赖于各个链之间的氢键相互作用，而且依赖于所得折叠扭曲、凸起和折叠成多面大分子构象的能力。因此，氨基酸倾向已被证明是高度依赖于上下文的，大大复杂的肽和蛋白质的设计富含{β}-结构。然而，最大的问题是分子间的相互作用，它损害了溶解性，这是许多淀粉样疾病的臭名昭著的特征。作者已经利用淀粉样肽自缔合的能量学构建嵌段共聚物，所述嵌段共聚物由来自β-淀粉样肽的中心结构域在C-末端与聚（乙二醇）缀合组成，1。本文使用小角中子散射（SANS）和电子显微镜（EM）来证明PEG嵌段在原纤维表面上的位置和布置，以确保原纤维共聚物的溶解性。
{beta}-sheet secondary structure is energetically dependent not only on the H-bonding interactions between individual strands, but also on the ability of the resulting sheet to twist, bulge, and fold into multifaceted macromolecular conformations. Consequently, amino acid propensities have proven to be highly context-dependent, greatly complicating the design of peptides and proteins rich in {beta}-structure. Most problematic, however, are the intermolecular interactions which compromise solubility, the infamous feature of the many amyloid diseases. The authors have exploited the energetics of self-association of amyloid peptides in the construction of a block copolymer consisting of the central domain from the {beta}-amyloid peptide conjugated with poly(ethylene glycol) at the C-terminus, 1. This paper uses small angle neutron scattering (SANS) and electron microscopy (EM), to demonstrate the location and disposition of the PEG block to be on the surface of the fibril, ensuring the solubility of the fibrillar copolymer.