Enhancing the Carboxylation Efficiency of Silk Fibroin through the Disruption of Noncovalent Interactions
Enhancing the Carboxylation Efficiency of Silk Fibroin through the Disruption of Noncovalent Interactions
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DOI：
10.1021/acs.bioconjchem.0c00168
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发表时间：
2020-05-01
影响因子：
4.7
通讯作者：
Burke, Kelly A.
中科院分区：
文献类型：
--
作者：
Heichel, Danielle L.;Burke, Kelly A.
丝素蛋白是用作可再生聚合物来源和生物材料平台的半结晶蛋白质，但现有的合成修饰丝素蛋白的方法效率低，这会限制蛋白质的效用。这项工作报告了一个温和的合成，通过在反应过程中的非共价相互作用的破坏，在羧基化的结果增加了2倍。重要的是，丝纤蛋白保持其形成β-片层的能力，所述β-片层对于定制机械和降解性质以及对于使固体构建体（例如，膜和支架）不溶于水。增加羧基官能化提供了对蛋白质电荷的控制，这允许使用静电相互作用来定制小分子的装载和释放。在水性碳二亚胺偶联过程中非共价相互作用的破坏也显著提高了含有伯胺基团的分子的缀合效率，从而使得能够与生物分子（例如蛋白质和肽）高度官能化，用于生物材料应用。
Silk fibroin is a semicrystalline protein used as a renewable polymer source and as a biomaterial platform, but existing methods to synthetically modify fibroin suffer from low efficiencies that can limit the protein's utility. This work reports on a mild synthesis that results in a 2-fold increase in carboxylation through the disruption of noncovalent interactions during the reaction. Importantly, silk fibroin maintains its ability to form beta-sheets that are critical for tailoring mechanical and degradation properties, as well as for rendering solid constructs (e.g., films and scaffolds) insoluble in water. Increasing carboxyl functionalization affords control over protein charge, which permits tailoring the loading and release of small molecules using electrostatic interactions. Disruption of noncovalent interactions during aqueous carbodiimide coupling also significantly enhances conjugation efficiency of molecules containing primary amine groups, thus enabling high degrees of functionalization with biological molecules, such as proteins and peptides, for biomaterial applications.