Monomodal polyelectrolyte complex nanoparticles of PDADMAC/Poly(styrenesulfonate): preparation and protein interaction.
Monomodal polyelectrolyte complex nanoparticles of PDADMAC/Poly(styrenesulfonate): preparation and protein interaction.
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DOI：
10.1002/mabi.200600143
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发表时间：
2006-11
影响因子：
4.6
通讯作者：
W. Ouyang;M. Müller
中科院分区：
文献类型：
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作者：
W. Ouyang;M. Müller
报道了模型蛋白HSA、LYZ和MYO与PEC纳米颗粒的结合。将PDADMAC溶液与PSS或PMA-MS混合，连续离心，制备PEC颗粒。采用非化学计量混合比得到了单模阴离子（PEC-1.50）和阳离子（PEC-0.66）的PEC颗粒。将带电荷的蛋白质溶液加入到各自带电荷的PEC颗粒分散体中，然后离心一步，制备PEC/蛋白质偶联物。在有吸引力的条件下，将蛋白质和PEC颗粒混合会导致分散的絮凝。从CD、DLS和AFM得到了在排斥条件下PEC颗粒上蛋白质结合的趋势：HSA/PEC-1.50 > MYO/PEC-1.50 > LYZ/PEC-0.66。在c(PROT) = 0.091 mg时，蛋白质吸收量可达0.33 g × g(-1)（蛋白质/PEC） （CD），粒径扩大至13 nm （AFM）。毫升(1)。此外，新型自旋包覆的PEC粒子薄膜在排斥和吸引条件下与蛋白质相互作用。原位ATR - FT-IR光谱显示，在吸引条件下，HSA和LYZ的吸附量明显高于排斥条件下，这类似于以聚阳离子或聚阴离子终止的聚电解质多层膜上的蛋白质吸附。与分散的PEC/蛋白偶联物类似，在排斥条件下，HSA的摄取比LYZ高。在排斥条件下所显示的蛋白质摄取与非生物源底物的轻度酶或蛋白质结合的概念有关。
The binding of the model proteins HSA, LYZ and MYO to PEC nanoparticles is reported. PEC particles were prepared by mixing solutions of PDADMAC either with PSS or PMA-MS, followed by consecutive centrifugation. Monomodal anionic (PEC-1.50) and cationic (PEC-0.66) PEC particles were obtained using non-stoichiometric mixing ratios. PEC/protein conjugates were prepared by adding charged protein solutions to dispersions of respective like charged PEC particles, followed by one centrifugation step. Mixing proteins and PEC particles under attractive conditions led to flocculation of the dispersion. From CD, DLS and AFM the following trend for protein binding at PEC particles under repulsive conditions was obtained: HSA/PEC-1.50 > MYO/PEC-1.50 > LYZ/PEC-0.66. Protein uptakes up to 0.33 g x g(-1) (protein/PEC) (CD) and particle diameter enlargements up to 13 nm (AFM) were obtained at c(PROT) = 0.091 mg . mL(-1). Furthermore, novel spin coated films of PEC particles were interacted with proteins under both repulsive and attractive conditions. In-situ ATR FT-IR spectroscopy revealed that the adsorbed amount of HSA and LYZ under attractive conditions was significantly higher than under repulsive ones, which is analogous to protein adsorption at polyelectrolyte multilayers terminated either by polycation or polyanion. Similarly to the dispersed PEC/protein conjugates, under repulsive conditions the uptake of HSA was higher compared to LYZ. The shown protein uptake under repulsive conditions is related to concepts of mild enzyme or protein binding at nonbiogenic substrates.