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Anchored protease-activatable polymersomes for molecular diagnostics of metastatic cancer cells

Authors
 Hyun-Ouk Kim  ;  Jong-Woo Lim  ;  Jihye Choi  ;  Hwunjae Lee  ;  Hye Young Son  ;  Jihye Kim  ;  Geunseon Park  ;  Haejin Chun  ;  Daesub Song  ;  Yong-Min Huh  ;  Seungjoo Haam 
Citation
 Journal of Materials Chemistry B, Vol.5(48) : 9571-9578, 2017 
Journal Title
 Journal of Materials Chemistry B 
ISSN
 2050-750X 
Issue Date
2017
Abstract
Real-time quantitative and qualitative analyses of metastasis-associated proteases are critical for precise diagnosis and novel therapeutic treatment of advanced cancers. However, conventional methods based on DNA, peptides, and proteins require sophisticated chemistry and additional processes to expose detection moieties, and they lack elements of temporal control, which limit their applicability. We designed unique protease-activatable polymersomes (PeptiSomes) for high sensitivity, in situ quantitative analysis of activating membrane-type 1 matrix metalloproteinases (MT1-MMP, MMP14). To do this, we first synthesized an amphiphilic block polymer–peptide and a copolypeptide based on mPEG-b-pLeu and MT1-peptide-b-pLeu, respectively. Amphiphilic self-assembled PeptiSomes in water were capable of disassembling and releasing the encapsulated self-quenched fluorescence dye (calcein) via enzymatic activation by MT1-MMP. Our PeptiSome system may potentially prevent the initiation and progression of cancer metastasis. Furthermore, the PeptiSome approach described here is likely to facilitate the development of rapid protease assay techniques and further extend the role of proteases as metastasis indicators and therapeutic targets.
URI
http://ir.ymlib.yonsei.ac.kr/handle/22282913/161508
DOI
10.1039/C7TB01675A
Appears in Collections:
1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > BioMedical Science Institute (의생명과학부)
1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > Dept. of Radiology (영상의학교실)
Yonsei Authors
손혜영(Son, Hye Yeong)
최지혜(Choi, Jihye)
허용민(Huh, Yong Min)
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Full Text
http://pubs.rsc.org/en/content/articlelanding/2017/tb/c7tb01675a#!divAbstract
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