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Templated Collagen 'Double Helices' Maintain Their Structure

机译:模板化胶原蛋白“双螺旋”保持其结构

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摘要

The self-assembly of collagen-mimetic peptides (CMPs) that form sticky-ended triple helices has allowed the production of surprisingly stable artificial collagen fibers and hydrogels. Assembly through sticky ends requires the recognition of a single strand by a templated strand dimer. Although CMPs and their triple helices have been studied extensively, the structure of a strand dimer is unknown. Here, we evaluate the physical characteristics of such dimers, using disulfide-templated (PPG)_(10) dimers as a model. Such "linked-dimers" retain their collagen-like structure even in the absence of a third strand, but only when their strands are capable of adopting a triple-helical fold. The intrinsic collagen-like structure of templated CMP pairs helps to explain the success of sticky-ended CMP association and changes the conception of new synthetic collagen designs.
机译:形成粘性末端三重螺旋的模拟胶原蛋白肽(CMP)的自组装,可以生产出令人惊讶的稳定的人造胶原蛋白纤维和水凝胶。通过粘性末端组装需要模板链二聚体识别单链。尽管已广泛研究了CMP及其三重螺旋,但尚不知道链二聚体的结构。在这里,我们使用二硫键模板(PPG)_(10)二聚体作为模型来评估此类二聚体的物理特性。这样的“连接二聚体”即使在没有第三链的情况下也保持其胶原样结构,但是仅当它们的链能够采用三螺旋折叠时。模板化CMP对的固有胶原样结构有助于解释粘性末端CMP结合的成功,并改变了新的合成胶原设计的概念。

著录项

  • 来源
    《Journal of the American Chemical Society》 |2020年第3期|1137-1141|共5页
  • 作者单位

    Massachusetts Institute of Technology Cambridge Massachusetts and University of Wisconsin—Madison Madison Wisconsin;

    University of Wisconsin—Madison Madison Wisconsin;

    Massachusetts Institute of Technology Cambridge Massachusetts University of Wisconsin—Madison Madison Wisconsin;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

  • 入库时间 2022-08-18 05:13:25

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