Elastin-like polypeptides (ELPs) are being developed for numerous biomedical applications. There is a limited understanding of ELP biocompatibility, with conflicting results in the literature. Protein adsorption is the fate determining event for blood-contacting biomaterials. The aim of this study is to elucidate the biocompatibility of ELP-based nanoparticles by examining the adsorbed proteome from platelet poor human plasma as a function of the physicochemical properties of these nanoparticles: diameter, amino acid hydrophobicity, and chain length. It was found that all ELP constructs had adsorbed an extremely large amount of albumin and high levels of immunoglobulin G and activated complement factor 3. Variations in the compositions of the proteomes across the eight nanoparticle systems studied were observed for plasminogen, fibronectin, activated fibrinogen, and coagulation modulating antithrombin and alpha₂ macroglobulin. Plasma clotting experiments showed that ELP-based nanoparticles slightly inhibited normal blood clotting, with shorter and/or more hydrophilic constructs showing a greater difference from the control than longer or more hydrophobic constructs. These results indicate that ELP nanoparticles, regardless of chain length, particle diameter, or amino acid hydrophobicity, may have the potential to stimulate a humoral immune response via immunoglobulin G and activated complement factor 3 despite the large amounts of albumin adsorbed at the blood-material interface.

中文翻译：

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人血浆蛋白对弹性蛋白样多肽纳米颗粒的吸附

弹性蛋白样多肽（ELP）正在开发用于许多生物医学应用。对ELP生物相容性的了解有限，文献中的结果相互矛盾。蛋白质吸附是血液接触生物材料的命运决定因素。这项研究的目的是通过检查贫血小板人血浆中吸附的蛋白质组与这些纳米粒子的物理化学特性（直径，氨基酸疏水性和链长）的关系，阐明基于ELP的纳米粒子的生物相容性。结果发现，所有ELP构建体均吸附了大量白蛋白，高水平的免疫球蛋白G和活化的补体因子3。在研究的8个纳米颗粒系统中，蛋白质组蛋白的组成存在纤溶酶原，纤连蛋白，₂巨球蛋白。血浆凝结实验表明，基于ELP的纳米颗粒略微抑制了正常血液凝结，与更长或更疏水的构建体相比，较短和/或更亲水的构建体显示出与对照的更大差异。这些结果表明，尽管有大量白蛋白吸附在血液材料上，但无论链长，粒径或氨基酸疏水性如何，ELP纳米颗粒都可能具有通过免疫球蛋白G和活化的补体因子3刺激体液免疫反应的潜力。接口。