Malik Shahid A, Mondal Somnath, Atreya Hanudatta S
Department of Solid State and Structural Chemistry Unit, NMR Research Centre, Indian Institute of Science Bangalore-560012 India
RSC Adv. 2019 Sep 12;9(49):28746-28753. doi: 10.1039/c9ra05514b. eCollection 2019 Sep 9.
Intrinsically disordered proteins (IDPs), being sensitive to proteolytic degradation both and , 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.
内在无序蛋白（IDP）对蛋白水解降解敏感，可通过与各种结合伴侣的相互作用而稳定。在此，我们首次表明银纳米颗粒（AgNP）有能力延长一种IDP的半衰期，从而使其在蛋白水解降解作用下稳定一个月。利用二维核磁共振光谱和其他生物物理技术研究了人胰岛素样生长因子结合蛋白-2（L-hIGFBP2）的无结构连接域与10纳米柠檬酸盐包覆的AgNP的共轭物。我们的研究揭示了该IDP与AgNP之间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中易被蛋白水解的位点并使其稳定。这项研究为设计靶向IDP的合适纳米颗粒以及以稳定形式将IDP储存、稳定并递送至细胞开辟了新途径。
