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A Vesicle Supra‐Assembly Approach to Synthesize Amine‐Functionalized Hollow Dendritic Mesoporous Silica Nanospheres for Protein Delivery
Author(s) -
Meka Anand Kumar,
Abbaraju Prasanna Lakshmi,
Song Hao,
Xu Chun,
Zhang Jun,
Zhang Hongwei,
Yu Meihua,
Yu Chengzhong
Publication year - 2016
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201602052
Subject(s) - mesoporous silica , vesicle , intracellular , amine gas treating , cationic polymerization , mesoporous material , chemistry , covalent bond , chemical engineering , calcination , biophysics , materials science , nanotechnology , membrane , catalysis , biochemistry , polymer chemistry , organic chemistry , biology , engineering
Intracellular delivery of proteins is a promising strategy of intervention in disease, which relies heavily on the development of efficient delivery platforms due to the cell membrane impermeability of native proteins, particularly for negatively charged large proteins. This work reports a vesicle supra‐assembly approach to synthesize novel amine‐functionalized hollow dendritic mesoporous silica nanospheres (A‐HDMSN). An amine silica source is introduced into a water–oil reaction solution prior to the addition of conventional silica source tetraethylorthosilicate. This strategy favors the formation of composite vesicles as the building blocks which further assemble into the final product. The obtained A‐HDMSN have a cavity core of ≈170 nm, large dendritic mesopores of 20.7 nm in the shell and high pore volume of 2.67 cm 3 g −1 . Compared to the calcined counterpart without amine groups (C‐HDMSN), A‐HDMSN possess enhanced loading capacity to large negative proteins (IgG and β ‐galactosidase) and improved cellular uptake performance, contributed by the cationic groups. A‐HDMSN enhance the intracellular uptake of β ‐galactosidase by up to 5‐fold and 40‐fold compared to C‐HDMSN and free β ‐galactosidase, respectively. The active form of β ‐galactosidase delivered by A‐HDMSN retains its intracellular catalytic functions.