过氧化物酶催化近距离标记研究巨噬细胞介导内化过程中纳米材料-细胞界面的蛋白质组。

IF 10.9 1区 材料科学 Q1 CHEMISTRY, MULTIDISCIPLINARY
Nano Today Pub Date : 2025-12-01 Epub Date: 2025-08-09 DOI:10.1016/j.nantod.2025.102865
Yushuang Wei, Xiangyang Li, Yao Gong, Yue-Xuan Li, Jibin Guan, Bing Yuan, Yue Chen, Hong-Bo Pang
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引用次数: 0

摘要

纳米材料通常需要与质膜上的蛋白质相互作用才能交叉并进入细胞内目标。因此,为了充分了解细胞进入机制,全面了解纳米材料与细胞接触时界面上的蛋白质组是至关重要的。在这里,我们报道了一种基于过氧化物酶的接近标记方法来研究纳米颗粒(NP)-细胞界面上的蛋白质组。辣根过氧化物酶(HRP)与多种NP和其他配体类型结合,同时仍然能够生物素化NP(或配体)-受体复合物周围的蛋白质。使用两种基于NP的巨噬细胞症(MP)示踪剂,研究人员进行了蛋白质组学调查,揭示了传统和受体依赖性MP之间的界面蛋白质组差异。此外,我们的研究发现,e -钙粘蛋白(CDH1)虽然不是主要受体,但存在于np -细胞界面,对细胞摄取多种np具有重要的功能。总的来说,通过纳米技术与接近标记的结合,我们的研究为研究NP和大分子内化进入细胞的分子机制提供了一种绘制NP-细胞界面蛋白质组的方法。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Peroxidase-catalyzed proximity labeling to survey the proteome of nanomaterial-cell interface during macropinocytosis-mediated internalization.

Nanomaterials often need to interact with proteins on the plasma membrane to get cross and access their intracellular targets. Therefore, to fully understand the cell entry mechanism, it is of vital importance to gain a comprehensive insight into the proteome at the interface when nanomaterials encounter the cells. Here, we reported a peroxidase-based proximity labeling method to survey the proteome at the nanoparticle (NP)-cell interface. Horseradish peroxidase (HRP) was conjugated to a variety of NPs and other ligand types while still being able to biotinylate the proteins surrounding NP (or ligand)-receptor complexes. Using two NP-based tracers for macropinocytosis (MP), which is highly relevant to NP internalization, we performed a proteomic survey and revealed the interface proteome difference between traditional and receptor-dependent MP. Moreover, our survey found that E-cadherin (CDH1), while not serving as the primary receptor, is present at the NP-cell interface and is functionally important for the cellular uptake of a wide variety of NPs. Overall, by integrating nanotechnology with proximity labeling, our study provides an approach to map the proteome of NP-cell interface for investigating the molecular mechanism of NP and macromolecule internalization into cells.

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来源期刊
Nano Today
Nano Today 工程技术-材料科学:综合
CiteScore
21.50
自引率
3.40%
发文量
305
审稿时长
40 days
期刊介绍: Nano Today is a journal dedicated to publishing influential and innovative work in the field of nanoscience and technology. It covers a wide range of subject areas including biomaterials, materials chemistry, materials science, chemistry, bioengineering, biochemistry, genetics and molecular biology, engineering, and nanotechnology. The journal considers articles that inform readers about the latest research, breakthroughs, and topical issues in these fields. It provides comprehensive coverage through a mixture of peer-reviewed articles, research news, and information on key developments. Nano Today is abstracted and indexed in Science Citation Index, Ei Compendex, Embase, Scopus, and INSPEC.
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