Layer-by-layer assembly of hierarchical nanoarchitectures to enhance the systemic performance of nanoparticle albumin-bound paclitaxel
- Authors
- Ruttala, Hima Bindu; Ramasamy, Thiruganesh; Shin, Beom Soo; Choi, Han-Gon; Yong, Chul Soon; Kim, Jong Oh
- Issue Date
- Mar-2017
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- Albumin; Nanoparticle; Colloidal stability; Systemic performance; Breast cancer
- Citation
- INTERNATIONAL JOURNAL OF PHARMACEUTICS, v.519, no.1-2, pp.11 - 21
- Indexed
- SCIE
SCOPUS
- Journal Title
- INTERNATIONAL JOURNAL OF PHARMACEUTICS
- Volume
- 519
- Number
- 1-2
- Start Page
- 11
- End Page
- 21
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/10087
- DOI
- 10.1016/j.ijpharm.2017.01.011
- ISSN
- 0378-5173
- Abstract
- Although protein-bound paclitaxel (PTX, Abraxane (R)) has been established as a standard PTX-based therapy against multiple cancers, its clinical success is limited by unfavorable pharmacokinetics, suboptimal biodistribution, and acute toxicities. In the present study, we aimed to apply the principles of a layer-by-layer(LbL) technique to improve the poor colloidal stability and pharmacokinetic pattern of nanoparticle albumin-bound paclitaxel (nab-PTX). LbL-based nab-PTX was successfully fabricated by the alternate deposition of polyarginine (pARG) and poly(ethylene glycol)-block-poly(L-aspartic acid) (PEGb-PLD) onto an albumin conjugate. The presence of protective entanglement by polyamino acids prevented the dissociation of nab-PTX and improved its colloidal stability even at a 100-fold dilution. The combined effect of high nanoparticle internalization and controlled release of PTX from LbL-nab-PTX increased its cytotoxicity in MCF-7 and MDA-MB-231 breast cancer cells. LbL-nab-PTX consistently induced apoptosis in approximately 52% and 22% of MCF-7 and MDA-MB-231 cancer cells, respectively. LbL assembly of polypeptides effectively prevented exposure of PTX to the systemic environment and thereby inhibited drug-induced hemolysis. Most importantly, LbL assembly of polypeptides to nab-PTX effectively increased the blood circulation potential of PTX and improved therapeutic efficacy via a significantly higher area under the curve (AUC)(0-infinity). We report for the first time the application of LbL functional architectures for improving the systemic performance of nab-PTX with a view toward its clinical translation for cancer therapy. (C) 2017 Elsevier B.V. All rights reserved.
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