Unbiased Identification of the Liposome Protein Corona using Photoaffinity-based Chemoproteomics.,ACS Central Science

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Unbiased Identification of the Liposome Protein Corona using Photoaffinity-based Chemoproteomics.
ACS Central Science ( IF 12.7 ) Pub Date : 2020-04-01 , DOI: 10.1021/acscentsci.9b01222
Roy Pattipeiluhu ₁ , Stefan Crielaard ₁ , Iris Klein-Schiphorst ₁ , Bogdan I Florea ₂ , Alexander Kros ₁ , Frederick Campbell ₁

Affiliation

Protein adsorption to the surface of a nanoparticle can fundamentally alter the character, behavior, and fate of a nanoparticle in vivo. Current methods to capture the protein corona rely on physical separation techniques and are unable to resolve key, individual protein-nanoparticle interactions. As a result, the precise link between the "synthetic" and the "biological" identity of a nanoparticle remains unclear. Herein, we report an unbiased photoaffinity-based approach to capture, characterize, and quantify the protein corona of liposomes in their native state. Compared to conventional methods, our photoaffinity approach reveals markedly different interacting proteins as well as reduced total protein binding to liposome surfaces. Identified proteins do not follow protein abundancy patterns of human serum, as has been generally reported, but are instead dominated by soluble apolipoproteins-endogenous serum proteins that have evolved to recognize the lipidic surface of circulating lipoproteins. We believe our findings are the most accurate characterization of a liposome's biological identity but, more fundamentally, reveal liposome-protein binding is, in many cases, significantly less complex than previously thought.

中文翻译：

使用基于光亲和力的化学蛋白质组学对脂质体蛋白冠的无偏鉴定。

蛋白质吸附到纳米粒子的表面可以从根本上改变纳米粒子在体内的特性，行为和命运。当前捕获蛋白质电晕的方法依赖于物理分离技术，无法解决关键的，个别的蛋白质-纳米粒子相互作用。结果，纳米颗粒的“合成”身份和“生物学”身份之间的精确联系仍然不清楚。本文中，我们报告了一种基于无偏光亲和力的方法来捕获，表征和量化脂质体天然状态下的蛋白质电晕。与常规方法相比，我们的光亲和性方法揭示了相互作用的蛋白质明显不同，以及减少了总蛋白与脂质体表面的结合。鉴定出的蛋白质不符合人类血清中蛋白质的丰度模式，如通常所报道的那样，但是相反，它们已经被可溶性载脂蛋白-内源性血清蛋白所支配，该蛋白已经进化为识别循环脂蛋白的脂质表面。我们相信我们的发现是对脂质体生物学特性最准确的表征，但从根本上讲，在许多情况下，脂质体与蛋白质的结合比以前认为的复杂得多。

更新日期：2020-04-23

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