Enzymatic activation of cell-penetrating peptides in self-assembled nanostructures triggers fibre-to-micelle morphological transition. Issue 52 (14th June 2017)

• Record Type: Journal Article
• Authors: Shi, Yejiao; Hu, Yang; Ochbaum, Guy; Lin, Ran; Bitton, Ronit; Cui, Honggang; Azevedo, Helena S.
• Is Part Of: Chemical communications. Volume 53:Issue 52(2017)
• Page Start: 7037
• Page End: 7040
• Publication Date: 2017-06-14
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c7cc03512h
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Enzyme-assisted fibre-to-micelle transition in self-assembled nanostructures controls presentation of cell-penetrating peptides. Abstract : We report here a proof-of-concept design of a multi-domain cell-penetrating peptide amphiphile (CPPA) which can self-assemble into fibrous nanostructures and transform into spherical micelles upon enzymatic degradation by matrix metalloproteinase-2 (MMP-2) up-regulated in the tumour environment. Concomitant with this morphological transition, the cell-penetrating peptide (CPP), which was previously buried inside the CPPA fibers, could be presented on the surface of the CPPA micelles, enhancing their cell-penetrating ability. These multifunctional and enzyme-responsive CPP nanostructures hold potential as nanocarriers for tumour-targeted intracellular delivery of therapeutic and diagnostic agents.