Peptides that anneal to natural collagen in vitro and ex vivo.

Peptides that anneal to natural collagen in vitro and ex vivo.
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DOI:
10.1039/c2ob25190f
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发表时间:
2012-08-14
影响因子:
3.2
通讯作者:
Raines RT
Raines RT
中科院分区:
化学3区
文献类型:
--
作者:
Chattopadhyay S;Murphy CJ;McAnulty JF;Raines RT

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胶原蛋白占人体蛋白质的1/4,占人体皮肤干重的3/4。在这里,我们实施最近发现的结构和稳定性的胶原蛋白三螺旋设计新的化学形式,锚到天然胶原蛋白。关键成分是胶原蛋白模拟肽(CMP),其不能自组装成同源三聚体三螺旋,但能够自发退火至天然胶原蛋白。我们表明,这样的CMP含有4-氟脯氨酸残基,特别是,紧密结合哺乳动物胶原蛋白在体外和小鼠伤口离体。这些合成肽,加上染料或生长因子,可能预示着评估或治疗伤口的新时代。
Collagen comprises ¼ of the protein in humans and ¾ of the dry weight of human skin. Here, we implement recent discoveries about the structure and stability of the collagen triple helix to design new chemical modalities that anchor to natural collagen. The key components are collagen mimetic peptides (CMPs) that are incapable of self-assembly into homotrimeric triple helices, but are able to anneal spontaneously to natural collagen. We show that such CMPs containing 4-fluoroproline residues, in particular, bind tightly to mammalian collagen in vitro and to a mouse wound ex vivo. These synthetic peptides, coupled to dyes or growth factors, could herald a new era in assessing or treating wounds.
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