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Molecularly Imprinted Nanogels Acquire Stealth In Situ by Cloaking Themselves with Native Dysopsonic Proteins
Author(s) -
Takeuchi Toshifumi,
Kitayama Yukiya,
Sasao Reo,
Yamada Takuya,
Toh Kazuko,
Matsumoto Yu,
Kataoka Kazunori
Publication year - 2017
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201700647
Subject(s) - nanocarriers , albumin , chemistry , in vivo , biophysics , molecular imprinting , förster resonance energy transfer , serum albumin , blood proteins , fluorescein , drug delivery , fluorescence , biochemistry , biology , organic chemistry , selectivity , physics , microbiology and biotechnology , quantum mechanics , catalysis
Abstract Protein corona formation was regulated on the surface in vivo by molecular imprinting to enable polymeric nanogels to acquire stealth upon intravenous administration. Albumin, the most abundant protein in blood, was selected as a distinct protein component of protein corona for preparing molecularly imprinted nanogels (MIP‐NGs) to form an albumin‐rich protein corona. Intravital fluorescence resonance energy transfer imaging of rhodamine‐labeled albumin and fluorescein‐conjugated MIP‐NGs showed that albumin was captured by MIP‐NGs immediately after injection, forming an albumin‐rich protein corona. MIP‐NGs circulated in the blood longer than those of non‐albumin‐imprinted nanogels, with almost no retention in liver tissue. MIP‐NGs also passively accumulated in tumor tissue. These data suggest that this strategy, based on regulation of the protein corona in vivo, may significantly influence the development of drug nanocarriers for cancer therapy.