Westermark Per, Lundmark Katarzyna, Westermark Gunilla T
Rudbeck Laboratory, Department of Genetics and Pathology, Uppsala University, Uppsala, Sweden.
PLoS One. 2009 Jun 30;4(6):e6041. doi: 10.1371/journal.pone.0006041.
Mouse AA-amyloidosis is a transmissible disease by a prion-like mechanism where amyloid fibrils act by seeding. Synthetic peptides with no amyloid relationship can assemble into amyloid-like fibrils and these may have seeding capacity for amyloid proteins.
Several synthetic peptides, designed for nanotechnology, have been examined for their ability to produce fibrils with Congo red affinity and concomitant green birefringence, affinity for thioflavin S and to accelerate AA-amyloidosis in mice. It is shown that some amphiphilic fibril-forming peptides not only produced Congo red birefringence and showed affinity for thioflavin S, but they also shortened the lag phase for systemic AA-amyloidosis in mice when they were given intravenously at the time of inflammatory induction with silver nitride. Peptides, not forming amyloid-like fibrils, did not have such properties.
These observations should caution researchers and those who work with synthetic peptides and their derivatives to be aware of the potential health concerns.
小鼠AA淀粉样变性是一种通过朊病毒样机制传播的疾病，其中淀粉样原纤维通过播种起作用。与淀粉样蛋白无关的合成肽可以组装成淀粉样蛋白样原纤维，并且这些原纤维可能对淀粉样蛋白具有播种能力。
已经检测了几种为纳米技术设计的合成肽产生具有刚果红亲和力和伴随的绿色双折射的原纤维的能力、对硫黄素S的亲和力以及在小鼠中加速AA淀粉样变性的能力。结果表明，一些两亲性成纤维肽不仅产生刚果红双折射并显示出对硫黄素S的亲和力，而且当它们在氮化银诱导炎症时静脉内给药时，还缩短了小鼠全身性AA淀粉样变性的延迟期。不形成淀粉样蛋白样原纤维的肽不具有这些特性。
这些观察结果应提醒研究人员以及使用合成肽及其衍生物的人员注意潜在的健康问题。
