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Molecules 2016, 21(11), 1457; doi:10.3390/molecules21111457

Mono-PEGylation of Alpha-MMC and MAP30 from Momordica charantia L.: Production, Identification and Anti-Tumor Activity

School of Medical Laboratory Science, Chengdu Medical College, Chengdu 610500, Sichuan, China
The First Affiliated Hospital of Chengdu Medical College, Chengdu 610000, Sichuan, China
Key Laboratory of Bio-Resources and Eco-Environment Ministry of Education/Animal Disease Prevention and Food Safety Key Laboratory of Sichuan Province, College of Life Science, Sichuan University, Chengdu 610064, Sichuan, China
Author to whom correspondence should be addressed.
Academic Editor: Els Van Damme
Received: 20 September 2016 / Revised: 29 October 2016 / Accepted: 29 October 2016 / Published: 31 October 2016
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PEGylation is a well-established and effective strategy to decrease immunogenicity, which can increase the stability and in vivo half-life time. However, the generation of multi-site modified products is inevitable due to the lysine chemistry, which will bring difficulties in subsequent research, such as purification and quantification. Site-specific modification by mPEG-succinimidyl carbonate (mPEG-SC) is a widely used method for N-terminal conjugation. In this study, we used it for site-directed modification on two ribosome-inactivating proteins (RIPs), alpha-momorcharin (α-MMC) and momordica anti-HIV protein (MAP30), from Momordica charantia L. According to the optimization of previous modification conditions, we compared Macro-Cap SP with SP-Sepharose FF chromatography for separating the final mPEGylated RIPs. Two kinds of methods both can obtain homogenous mPEGylated RIPs which were identified by sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS-PAGE), isoelectric focusing electrophoresis (IEF), and matrix-assisted laser desorption ionization-time of flight/time of flight (MALDI-TOF/TOF) analysis. We also used iodine staining method to detect the amount of unmodified PEG. Furthermore, the inhibition activity of both mPEGylated and non-PEGylated RIPs against human lung adenocarcinoma epithelial A549 cells was detected. All of the results suggested that the mPEGylated α-MMC/MAP30 might be potentially developed as new anti-tumor drugs. View Full-Text
Keywords: ribosome-inactivating protein; alpha-momorcharin (α-MMC); momordica anti-HIV protein (MAP30); protein PEGylation; anti-tumor ribosome-inactivating protein; alpha-momorcharin (α-MMC); momordica anti-HIV protein (MAP30); protein PEGylation; anti-tumor

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Sun, Y.; Sun, F.; Li, J.; Wu, M.; Fan, X.; Meng, Y.; Meng, Y. Mono-PEGylation of Alpha-MMC and MAP30 from Momordica charantia L.: Production, Identification and Anti-Tumor Activity. Molecules 2016, 21, 1457.

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