A novel insight into mechanism of derangement of coagulation balance: interactions of quantum dots with coagulation-related proteins.
A novel insight into mechanism of derangement of coagulation balance: interactions of quantum dots with coagulation-related proteins.
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对凝血平衡紊乱机制的新见解：量子点与凝血相关蛋白的相互作用
DOI：
10.1186/s12989-022-00458-x
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发表时间：
2022-03-08
影响因子：
10
通讯作者：
Huang P
中科院分区：
文献类型：
--
作者：
Zhang L;Wu Y;Luo X;Jia T;Li K;Zhou L;Mao Z;Huang P
量子点因其广泛的生物医学和电子产品应用而受到越来越多的关注。由于量子点在接触循环系统方面的高度优先性，了解量子点的血液相容性是其生物安全性评价的最重要方面之一。到目前为止，量子点对凝血平衡的影响尚未完全了解，有限的研究也尚未从量子点与凝血相关蛋白的相互作用的角度阐明潜在的机制。QDs通过延长活化部分凝血活酶时间和凝血酶原时间以及改变凝血和纤溶因子的表达水平，导致凝血平衡紊乱。QDs与凝血和纤溶系统中主要的凝血相关蛋白PTM（prothrombin）、PLG（plasminogen）和FIB（fibrinogen）通过氢键和疏水作用形成QDs-蛋白缀合物。蛋白质与量子点的亲和力顺序为PTM > PLG > FIB，与CdTe/ZnS量子点的亲和力大于与CdTe量子点的亲和力。量子点与PTM、PLG和FIB的结合不仅引起它们的荧光猝灭，而且改变了它们的构象结构。量子点与PTM、PLG和FIB活性位点的结合可促进蛋白质的活化，从而干扰止血和纤溶过程。量子点与PTM、PLG和FIB的相互作用可能是干扰凝血平衡的关键因素，这有助于从分子水平上对量子点的潜在生物学影响进行可靠和全面的评价。在线版本包含补充材料，可通过10.1186/s12989-022-00458-x获得。
Quantum dots (QDs) have gained increased attention for their extensive biomedical and electronic products applications. Due to the high priority of QDs in contacting the circulatory system, understanding the hemocompatibility of QDs is one of the most important aspects for their biosafety evaluation. Thus far, the effect of QDs on coagulation balance haven’t been fully understood, and limited studies also have yet elucidated the potential mechanism from the perspective of interaction of QDs with coagulation-related proteins. QDs induced the derangement of coagulation balance by prolonging the activated partial thromboplastin time and prothrombin time as well as changing the expression levels of coagulation and fibrinolytic factors. The contact of QDs with PTM (prothrombin), PLG (plasminogen) and FIB (fibrinogen) which are primary coagulation-related proteins in the coagulation and fibrinolysis systems formed QDs-protein conjugates through hydrogen-bonding and hydrophobic interaction. The affinity of proteins with QDs followed the order of PTM > PLG > FIB, and was larger with CdTe/ZnS QDs than CdTe QDs. Binding with QDs not only induced static fluorescence quenching of PTM, PLG and FIB, but also altered their conformational structures. The binding of QDs to the active sites of PTM, PLG and FIB may promote the activation of proteins, thus interfering the hemostasis and fibrinolysis processes. The interactions of QDs with PTM, PLG and FIB may be key contributors for interference of coagulation balance, that is helpful to achieve a reliable and comprehensive evaluation on the potential biological influence of QDs from the molecular level. The online version contains supplementary material available at 10.1186/s12989-022-00458-x.
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影响因子：
4.6
作者：
Huang H;Lai W;Cui M;Liang L;Lin Y;Fang Q;Liu Y;Xie L
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DOI：
10.1016/j.saa.2015.04.106
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