Assessing the Potential of Folded Globular Polyproteins As Hydrogel Building Blocks.
Assessing the Potential of Folded Globular Polyproteins As Hydrogel Building Blocks.
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DOI：
10.1021/acs.biomac.6b01877
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发表时间：
2017-02-13
影响因子：
6.2
通讯作者：
Dougan L
中科院分区：
文献类型：
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作者：
da Silva MA;Lenton S;Hughes M;Brockwell DJ;Dougan L
蛋白质的天然状态通常具有稳定的明确的折叠结构，赋予这些生物分子特定的功能和分子识别能力。在这里，我们探索使用折叠的球状多聚蛋白作为水凝胶的构建块的潜力。光化学交联的水凝胶由含有I27（（I27）5）、蛋白L（（pL）5）或这些蛋白的1：1共混物的五个结构域的多蛋白产生。小角X射线散射分析表明（I27）5以单一棒状结构存在，而（pL）5在溶液中显示出自聚集的特征。SANS测量表明，两种多蛋白水凝胶具有相似的纳米级结构，其中蛋白L水凝胶由更小和更紧凑的簇形成。多蛋白水凝胶在加载/卸载循环中显示出小的能量耗散，当水凝胶在未折叠状态下形成时，能量耗散显著增加。这项研究证明了使用折叠蛋白质作为水凝胶中的构建块，并强调了潜在的多功能性，可以提供在调整多聚蛋白的机械，结构和功能特性。
The native states of proteins generally have stable well-defined folded structures endowing these biomolecules with specific functionality and molecular recognition abilities. Here we explore the potential of using folded globular polyproteins as building blocks for hydrogels. Photochemically cross-linked hydrogels were produced from polyproteins containing either five domains of I27 ((I27)5), protein L ((pL)5), or a 1:1 blend of these proteins. SAXS analysis showed that (I27)5 exists as a single rod-like structure, while (pL)5 shows signatures of self-aggregation in solution. SANS measurements showed that both polyprotein hydrogels have a similar nanoscopic structure, with protein L hydrogels being formed from smaller and more compact clusters. The polyprotein hydrogels showed small energy dissipation in a load/unload cycle, which significantly increased when the hydrogels were formed in the unfolded state. This study demonstrates the use of folded proteins as building blocks in hydrogels, and highlights the potential versatility that can be offered in tuning the mechanical, structural, and functional properties of polyproteins.