Protein diffusion in agarose hydrogel in situ measured by improved refractive index method
Protein diffusion in agarose hydrogel in situ measured by improved refractive index method
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通过改进的折射率法原位测量琼脂糖水凝胶中的蛋白质扩散
DOI：
10.1016/j.jconrel.2006.08.006
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发表时间：
2006-10-10
影响因子：
10.8
通讯作者：
Zhang, Lina
中科院分区：
文献类型：
--
作者：
Liang, Songmiao;Xu, Jian;Zhang, Lina
准确了解蛋白质在仿生水凝胶基质中在体温下的扩散行为对于设计高效的基于蛋白质的药物控释装置具有重要意义。本文改进了已有的原位折射率法，使其具有很强的温度控制能力。首次采用这种新改进的方法研究了蛋白质（牛血清白蛋白（BSA）和溶菌酶）在琼脂糖水凝胶中在体温（37 ℃）下的扩散。在扩散过程中，由凝胶内扩散蛋白质浓度的变化引起的凝胶折射率的变化使得能够估计蛋白质的有效扩散系数。蛋白质的扩散系数随琼脂糖浓度的增加和溶质分子尺寸的增大而减小。在所考虑的琼脂糖浓度范围（0.5-3.0重量%）下，BSA和溶菌酶的扩散系数分别为4.98 ~ 8.21 × 10 ~（-7）cm ~（2）/s和1.15 ~ 1.56 × 10 ~（-6）cm ~（2）/s。研究了BSA在琼脂糖凝胶中的扩散系数随温度的变化规律。此外，聚合物的体积分数对BSA和溶菌酶在琼脂糖水凝胶中的扩散的阻滞效应进行了分析，三个模型，Amsden的，Clauge和Philips的，和Ogsten的模型。(c)2006 Elsevier B. V.保留所有权利。
The accurate knowledge of the diffusion behavior of protein within biomimetic hydrogel matrix at body temperature has a great implication for the design of efficient controlled release protein-base drug delivery devices. In this paper, we improved our previous in situ refractive index method with great temperature-controlled capability. For the first time, this newly improved method was employed to study the diffusion of protein (bovine serum albumin (BSA) and lysozyme) in agarose hydrogel at body temperature (37 degrees C). The change of the gel refractive index caused by the change of the diffusing protein concentration within the gel during the diffusion process enables the effective diffusion coefficients of protein to be estimated. The diffusion coefficients of proteins decrease with the increase of the concentration of agarose and the solute molecular size. At the considered range of agarose concentration (0.5-3.0 wt.%), the diffusion coefficients range from 4.98 to 8.21 X 10(-7) cm(2)/s for BSA and 1.15 to 1.56 x 10(-6) cm(2)/s for lysozyme, respectively. Temperature dependence of diffusivity of BSA in agarose hydrogel was also investigated. Furthermore, the retardance effect of polymer volume fraction on the diffusivity of both BSA and lysozyme in agarose hydrogels was analyzed with three models, Amsden's, Clauge and Philips', and Ogsten's model. (c) 2006 Elsevier B.V. All rights reserved.