Comparative investigation on the sizes and scavenger receptor binding of human native and modified lipoprotein particles with atomic force microscopy.

Comparative investigation on the sizes and scavenger receptor binding of human native and modified lipoprotein particles with atomic force microscopy.
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用原子力显微镜比较研究人天然和修饰脂蛋白颗粒的尺寸和清道夫受体结合

DOI:
10.1186/s12951-018-0352-3
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发表时间:
2018-03-21
影响因子:
10.2
通讯作者:
Chen Y
Chen Y
中科院分区:
工程技术1区
文献类型:
--
作者:
Gan C;Wang K;Tang Q;Chen Y

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血浆脂蛋白的大小和受体结合能力与其结构/功能密切相关。目前,天然脂蛋白的大小已经通过包括原子力显微镜(AFM)在内的各种方法来测量,而修饰脂蛋白的大小却很难确定,脂蛋白的受体结合能力也很少在纳米尺度上被检测和比较。本研究利用原子力显微镜(AFM)检测和比较了三种天然人脂蛋白(高密度脂蛋白、低密度脂蛋白和极低密度脂蛋白)和两种修饰人脂蛋白(氧化和乙酰化LDL)的大小和清净受体结合特性,并分别以牛血清白蛋白及其抗体作为阴性和阳性对照。AFM检测到这些脂蛋白的大小接近于已知值和先前报道的AFM检测大小,并且天然LDL和修饰LDL具有不同的高度/大小。AFM还显示,5种脂蛋白的CD36结合能力彼此不同,与SR-B1的结合能力也不同,作为阳性对照的抗CD36/SR-B1抗体具有较强的CD36/SR-B1结合能力。这些数据为更好地了解脂蛋白的结构和功能提供了重要的信息。此外,数据证明,除了尺寸测量外,AFM还可以在纳米尺度上可视化受体-脂蛋白结合,以及抗原-抗体(清道夫受体及其抗体)结合。
The size and receptor-binding abilities of plasma lipoproteins are closely related with their structure/functions. Presently, the sizes of native lipoproteins have been measured by various methods including atomic force microscopy (AFM) whereas the sizes of modified lipoproteins are poorly determined and the receptor-binding ability of lipoproteins is less detected and compared at the nanoscale. Here, AFM was utilized to detect/compare the size and scavenger receptor-binding properties of three native human lipoproteins including high-density lipoprotein, low-density lipoprotein (LDL), and very low-density lipoprotein, and two modified human lipoproteins including oxidized and acetylated LDL, as well as bovine serum albumin and their antibodies as negative and positive controls, respectively. AFM detected that the sizes of these lipoproteins are close to the commonly known values and the previously-reported AFM-detected sizes and that native and modified LDL have different height/size. AFM also revealed that the CD36-binding abilities of the five lipoproteins are different from one another and from their SR-B1-binding abilities and that the anti-CD36/SR-B1 antibodies as positive controls have strong CD36/SR-B1-binding abilities. The data provide important information on lipoproteins for better understanding their structures/functions. Moreover, the data certify that besides size measurement AFM also can visualize receptor-lipoprotein binding at the nanoscale, as well as antigen–antibody (scavenger receptors and their antibodies) binding.
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