Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/95129
Title: Efficient intracellular delivery of functional proteins using cationic polymer core/shell nanoparticles
Authors: Lee, Ashlynn L. Z.
Wang, Yong
Ye, Wen-Hui
Yoon, Ho Sup
Chan, Sui Yung
Yang, Yi-Yan
Keywords: DRNTU::Engineering::Materials::Biomaterials
Issue Date: 2007
Source: Lee, A. L., Wang, Y., Ye, W. H., Yoon, H. S., Chan, S. Y., & Yang, Y. Y. (2008). Efficient intracellular delivery of functional proteins using cationic polymer core/shell nanoparticles. Biomaterials, 29(9), 1224-1232.
Series/Report no.: Biomaterials
Abstract: Cationic core/shell nanoparticles self-assembled from biodegradable, cationic and amphiphilic copolymer poly{N-methyldietheneaminesebacate)-co-[(cholesteryloxocarbonylamido ethyl) methyl bis(ethylene) ammonium bromide] sebacate}, P(MDS-co-CES), were fabricated and employed to deliver lectin A-chain, an anticancer glycoprotein. Lectin A-chain was efficiently bound onto the surfaces of the nanoparticles at high mass ratios of nanoparticles to lectin A-chain. The nanoparticle/lectin A-chain complexes had an average size of approximately 150 nm with zeta potential of about +30 mV at the mass ratio of 50 or above while the BioPorter/lectin A-chain complexes had a larger particle size and relatively lower zeta potential (150 nm vs. 455 nm; +30 mV vs. +20 mV). Therefore, the cellular uptake of nanoparticle/lectin A-chain com-plexes was much greater than that of BioPorter/lectin A-chain complexes. The results obtained from cytotoxicity tests show that lectin A-chain delivered by the nanoparticles was significantly more toxic against MDA-MB-231, HeLa, HepG2 and 4T1 cell lines when compared to Bio-Porter, and IC50 of lectin A-chain delivered by the nanoparticles was 0.2, 0.5, 10 and 50 mg/l, respectively, while that of lectin A-chain delivered by BioPorter was higher than 100 mg/l in all cell lines tested. These nano-sized particles may provide an efficient approach for intracellular delivery of biologically active proteins.
URI: https://hdl.handle.net/10356/95129
http://hdl.handle.net/10220/8522
ISSN: 01429612
DOI: http://dx.doi.org/10.1016/j.biomaterials.2007.11.021
Rights: © 2007 Elsevier Ltd. This is the author created version of a work that has been peer reviewed and accepted for publication by Biomaterials, Elsevier. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: http://dx.doi.org/10.1016/j.biomaterials.2007.11.021.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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