Pegylation enhances protein stability during encapsulation in PLGA microspheres

来自 NCBI

阅读量:

54

作者:

M DiwanTG Park

展开

摘要:

During encapsulation of proteins in biodegradable microspheres, a significant amount of the protein reportedly undergoes denaturation to form irreversible insoluble aggregates. Incomplete in vitro release of proteins from the microspheres is a common observation. An attempt was made to overcome this problem by pegylation of the protein to be encapsulated. Lysozyme, a model protein, was conjugated with methoxy polyethylene glycol (mPEG, MW 5000). The conjugate was characterized by SDS–PAGE, SE-HPLC, and MALDI–TOF mass spectroscopy. The pegylated lysozyme (Lys–mPEG) consisted of different isomers of mono-, di- and tri-pegylated with about 15% as native lysozyme. The specific activity of the protein was retained after pegylation (101.3±10.4%). The microsphere encapsulation process was simulated for pegylated and native lysozyme. Pegylated lysozyme exhibited much better stability than native lysozyme against exposure to organic solvent (dichloromethane), homogenization, and showed reduced adsorption onto the surface of blank PLGA microspheres. Release profiles of the two proteins from microspheres were very different. For native lysozyme, it was high initial release (about 50%) followed by a nearly no release (about 10% in 50 days). In contrast, Lys–mPEG conjugate showed a triphasic and near complete release over 83 days. This study shows that the pegylation of protein can provide substantial protection against the destabilization of protein during encapsulation.

展开

DOI:

10.1016/S0168-3659(01)00292-9

被引量:

354

年份:

2001

通过文献互助平台发起求助,成功后即可免费获取论文全文。

我们已与文献出版商建立了直接购买合作。

你可以通过身份认证进行实名认证,认证成功后本次下载的费用将由您所在的图书馆支付

您可以直接购买此文献,1~5分钟即可下载全文,部分资源由于网络原因可能需要更长时间,请您耐心等待哦~

身份认证 全文购买

相似文献

参考文献

引证文献

来源期刊

引用走势

2011
被引量:41

辅助模式

0

引用

文献可以批量引用啦~
欢迎点我试用!

引用