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Enhanced stability of an intrinsically disordered protein against proteolytic cleavage through interactions with silver nanoparticles

机译：通过与银纳米颗粒的相互作用增强了内在无序蛋白抵抗蛋白水解裂解的稳定性

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Intrinsically disordered proteins (IDPs), being sensitive to proteolytic degradation both in vitro and in vivo , can be stabilized by the interactions with various binding partners. Here, we show for the first time that silver nanoparticles (AgNPs) have the ability to enhance the half-life of an IDP, thereby rendering it stable for a month against proteolytic degradation. The conjugate of the unstructured linker domain of human insulin-like growth factor binding protein-2 (L-hIGFBP2) with 10 nm citrate-capped AgNPs was studied using two-dimensional NMR spectroscopy and other biophysical techniques. Our studies reveal the extent and nature of residue-specific interactions of the IDP with AgNPs. These interactions mask proteolysis-prone sites of the IDP and stabilize it. This study opens new avenues for the design of appropriate nanoparticles targeting IDPs and for storage, stabilization and delivery of IDPs into cells in a stable form.
机译：通过与各种结合配偶体的相互作用，可以稳定体内和体外对蛋白水解降解敏感的内在无序蛋白（IDP）。在这里，我们首次展示了纳米银颗粒（AgNPs）能够提高IDP的半衰期，从而使其在一个月内对蛋白水解降解保持稳定。使用二维NMR光谱和其他生物物理技术研究了人类胰岛素样生长因子结合蛋白2（L-hIGFBP2）的非结构化连接结构域与10 nm柠檬酸盐封端的AgNP的缀合物。我们的研究揭示了IDP与AgNPs残基特异性相互作用的程度和性质。这些相互作用掩盖了IDP易于蛋白水解的位点并使其稳定。这项研究为设计合适的针对IDP的纳米颗粒，以及以稳定的形式将IDP储存，稳定和递送到细胞中开辟了新途径。

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