Tunable, temperature-responsive polynorbornenes with side chains based on an elastin peptide sequence.
Tunable, temperature-responsive polynorbornenes with side chains based on an elastin peptide sequence.
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DOI：
10.1002/anie.200903888
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发表时间：
2009
影响因子：
16.6
通讯作者：
Grubbs, Robert H.
中科院分区：
文献类型：
--
作者：
Conrad, Rosemary M.;Grubbs, Robert H.
天然哺乳动物弹性蛋白纤维是蛋白质原弹性蛋白的交联网络，其作为人体血管的主要组分起作用。对这种蛋白质的广泛物理和理论研究揭示了其独特弹性背后的机制。[1]原弹性蛋白由重复氨基酸序列-（VPGVG）n-的疏水结构域和富含用于分子间交联的丙氨酸和赖氨酸残基的结构域组成。疏水结构域在构象上是动态的，并且在无规卷曲和紧密缠绕的β-折叠之间过渡，导致蛋白质的水化球发生大的变化。这个过程已被确定为交联网络的弹性的基础。[2]在没有链交联的情况下，构象变化表现为温度依赖性相变，称为低临界溶解温度（LCST），低于该温度蛋白质是可溶的，高于该温度蛋白质是不溶的。为了利用原弹性蛋白的物理性质，已经通过微生物表达系统合成了弹性蛋白样多肽（ELP）[3]，并且已经研究了其用作生物材料。[4]ELP所带来的希望激励我们寻找这些蛋白质的易于获得的合成衍生物，以开发促进内皮细胞生长的新材料。我们希望将弹性蛋白的氨基酸序列，-（VPGVG）-，作为侧链上的仿生聚乙烯，以获得一种合成的聚合物，表现出其多肽model.The的相变行为的货车Hest和卡梅隆组已经证明，与-（VPGVG）-弹性蛋白序列作为侧链的聚合物表现出LCST是依赖于浓度，聚合度和pH值。[5-6]使用受控自由基聚合方法合成聚合物以形成具有低聚合度（DP< 12）的阿坝嵌段共聚物[5]或具有较高DP的均聚物。[6]最近，Setton组已经表明，连接到异戊烯单体的-（VPGVG）-的二聚重复单元可以使用开环易位聚合（ROMP）以（H2 IMes）（PCy 3）Cl 2 Ru = CHPh作为引发剂进行聚合。所产生的低聚物（DP< 12）表现出温度依赖性相变。[七]《中国日报》
Natural mammalian elastin fibers are crosslinked networks of the protein tropoelastin, which functions as the primary component of human blood vessels. Extensive physical and theoretical studies on this protein have shed light on the mechanism behind its unique elasticity.[1] Tropoelastin is comprised of hydrophobic domains of the repeating amino acid sequence-(VPGVG) n-and domains rich in alanine and lysine residues for intermolecular crosslinking. The hydrophobic domains are conformationally dynamic and transition between random coils and tightly wound β-sheets, resulting in large changes in the hydration sphere of the protein. This process has been determined to be fundamental to the elasticity of the crosslinked networks.[2] In the absence of chain crosslinking, the conformation change is manifested by a temperature-dependent phase transition known as a lower critical solution temperature (LCST) below which the protein is soluble and above which it is insoluble. In order to take advantage of the physical properties of tropoelastin, elastin-like polypeptides (ELPs) have been synthesized by microbial expression systems [3] and have been studied for use as biomaterials.[4] The promise presented by ELPs has inspired us to search for readily accessible synthetic derivatives of these proteins for the development of new materials that promote endothelial cell growth. We hoped to incorporate the elastin amino acid sequence,-(VPGVG)-, as the side chain on biomimetic polynorbornenes to obtain a synthetic polymer that exhibits the phase transition behaviour of its polypeptide model.The van Hest and Cameron groups have demonstrated that polymers with the-(VPGVG)-elastin sequence as a side chain exhibit LCSTs that are dependent on concentration, degree of polymerization and pH.[5–6] The polymers were synthesized using controlled radical polymerization methods to form either ABA block copolymers with low degrees of polymerization (DP< 12)[5] or homopolymers with higher DPs.[6] Recently, the Setton group has shown that dimeric repeat units of-(VPGVG)-attached to norbornene monomers could be polymerized using ring-opening metathesis polymerization (ROMP) with (H2IMes)(PCy3) Cl2Ru= CHPh as an initiator. The oligomers (DP< 12) produced exhibited temperature dependent phase transitions.[7]
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影响因子：
15
作者：
Valiaev A;Lim DW;Schmidler S;Clark RL;Chilkoti A;Zauscher S
通讯作者：
Zauscher S
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影响因子：
15
作者：
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