CNRS UCBL, 7 passage du vercors, Lyon 69367 Cedex 07, France.
J Microencapsul. 2010;27(7):561-71. doi: 10.3109/02652048.2010.493620.
A study of the parameters relating to the preparation of para-acyl-calix[9]arene-based solid lipid nanoparticles (SLNs) has been undertaken. Dynamic light scattering and electron microscopy have shown that the particle size varies between 85 and 215 nm depending on the acyl chain length. Parameters, including the organic solvent, amphiphile concentration and the presence of a co-surfactant affect the size of the SLNs obtained significantly. In contrast, stirring speed and solution viscosity have no effect. The ionic strength of the suspension has been shown to affect SLN stability in a salt-dependent manner. Ultrasonic and ultraviolet and 80°C treatment of the SLN suspensions have no effect on the SLN stability. The SLNs are unstable with respect to freezing–defreezing cycles, but can be reconstituted using mono- or disaccharides as cryoprotectants. Importantly, the temporal stability of these suspensions in water has been shown to be superior to 6 months. With regard to protein interactions, no SLN aggregation was observed in the presence of human serum albumin, with formation of a monolayer of albumin on the surface of the SLNs. Encapsulation was shown using acridine as a fluorescent probe.
已经开展了与制备基于对酰基杯[9]芳烃的固体脂质纳米粒(SLN)相关参数的研究。动态光散射和电子显微镜显示,颗粒尺寸根据酰基链长度在 85 至 215nm 之间变化。包括有机溶剂、两亲物浓度和存在共表面活性剂在内的参数显著影响所获得的 SLN 的尺寸。相比之下,搅拌速度和溶液粘度对 SLN 的尺寸没有影响。已经表明悬浮液的离子强度以依赖于盐的方式影响 SLN 的稳定性。超声和紫外线以及 80°C 处理 SLN 悬浮液对 SLN 的稳定性没有影响。SLN 对冷冻-解冻循环不稳定,但可以使用单糖或二糖作为冷冻保护剂进行再构成。重要的是,这些悬浮液在水中的时间稳定性已被证明超过 6 个月。关于蛋白质相互作用,在存在人血清白蛋白的情况下未观察到 SLN 聚集,白蛋白在 SLN 的表面形成单层。使用吖啶作为荧光探针显示了包封。