Protein release from highly charged peptide hydrogel networks.
Protein release from highly charged peptide hydrogel networks.
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DOI：
10.1039/c5tb02137e
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发表时间：
2016-03-21
期刊：
影响因子：
--
通讯作者：
Schneider JP
中科院分区：
文献类型：
--
作者：
Nagy-Smith K ;Yamada Y ;Schneider JP
水凝胶是用于治疗性蛋白质的有用递送载体。控制蛋白质释放速率的能力对于凝胶的实用性至关重要，并且部分地定义了其临床应用。在封装的蛋白质和凝胶网络之间进行的静电相互作用代表了可以控制蛋白质运动的一种模式。对于许多凝胶，这种策略在低离子强度溶液条件下效果良好，但在生理相关离子强度的溶液中效果明显较差，其中静电相互作用更有效地被屏蔽。在本文中，我们发现高度带电的自组装肽可用于制备具有足够电势的纤维状水凝胶，以允许在生理缓冲液条件下基于静电控制蛋白质释放。流变学表明，蛋白质，在其等电点显着不同，可以直接封装在带负电荷或带正电荷的肽水凝胶网络在肽自组装事件导致凝胶化。与透射电子显微镜相结合的本体吸附研究表明，静电相互作用驱动蛋白质与最终凝胶状态中带相反电荷的原纤维的缔合，这反过来又决定了这些大分子在水凝胶网络中的扩散和保留。来自自组装肽的高电荷水凝胶网络允许在生理缓冲条件下基于静电控制蛋白质释放。
Hydrogels are useful delivery vehicles for therapeutic proteins. The ability to control the rate of protein release is paramount to a gel’s utility and, in part, defines its clinical application. Electrostatic interactions made between encapsulated protein and a gel’s network represents one modality in which protein motility can be controlled. For many gels this strategy works well under low ionic strength solution conditions, but dramatically less so in solutions of physiologically relevant ionic strength where electrostatic interactions are more effectively screened. Herein, we find that highly charged self-assembling peptides can be used to prepare fibrillar hydrogels of sufficient electropotential to allow electrostatic-based control over protein release under physiological buffer conditions. Rheology shows that proteins, differing significantly in their isoelectric point, can be directly encapsulated within negatively- or positively-charged peptide hydrogel networks during the peptide self-assembly event leading to gelation. Bulk adsorption studies coupled with transmission electron microscopy shows that electrostatic interactions drive the association of protein to oppositely charged fibrils in the final gel state, which in turn, dictates the diffusion and retention of these macromolecules in the hydrogel network. Highly charged hydrogel networks from self-assembling peptides allow electrostatic-based control over protein release under physiological buffer conditions.
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影响因子：
14
作者：
Branco, Monica C.;Pochan, Darrin J.;Wagner, Norman J.;Schneider, Joel P.
通讯作者：
Schneider, Joel P.
影响因子：
8.6
作者：
MACKINTOSH, FC;KAS, J;JANMEY, PA
通讯作者：
JANMEY, PA
影响因子：
8.6
作者：
Ozbas, B;Rajagopal, K;Pochan, DJ
通讯作者：
Pochan, DJ
影响因子：
14
作者：
Sinthuvanich, Chomdao;Haines-Butterick, Lisa A.;Nagy, Katelyn J.;Schneider, Joel P.
通讯作者：
Schneider, Joel P.
影响因子：
4.1
作者：
Bertz, Andreas;Woehl-Bruhn, Stefanie;Menzel, Henning
通讯作者：
Menzel, Henning