TY - JOUR
T1 - Stabilization of cancer-specific gene carrier via hydrophobic interaction for a clear-cut response to cancer signaling
AU - Kim, Chan Woo
AU - Toita, Riki
AU - Kang, Jeong Hun
AU - Li, Kai
AU - Lee, Eun Kyung
AU - Zhao, Guo Xi
AU - Funamoto, Daiki
AU - Nobori, Takanobu
AU - Nakamura, Yuta
AU - Mori, Takeshi
AU - Niidome, Takuro
AU - Katayama, Yoshiki
N1 - Funding Information:
We thank Professor Masahiro Goto (Kyushu University) for assistance in CLSM study. This work was financially supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan . C.W. Kim is grateful to the Japan Society for the Promotion of Science (JSPS) for the Dr. course scholarship.
PY - 2013
Y1 - 2013
N2 - Here, we developed a new gene carrier, comprising a linear polyethylenimine (LPEI) grafted with a hydro-phobically modified cationic peptide containing a long alkyl chain, for use in cancer-specific gene delivery. The cationic peptide is a substrate of protein kinase Cα (PKCα), which is known to be activated specifically in cancer cells. The hydrophobically modified LPEI-peptide conjugate (LPEI-C10-peptide) could form a polyplex with DNA through electrostatic and hydrophobic interactions between the anionic DNA strands and the cationic peptide substrate. The hydrophobic modification of the peptide did not affect the reactivity of the peptide toward PKCα, while the polyplex showed improved intracellular uptake. Because of the efficient endosomal escape and enhanced stability, the polyplex significantly improved the transgene regulation responding to intracellular PKCα activity.
AB - Here, we developed a new gene carrier, comprising a linear polyethylenimine (LPEI) grafted with a hydro-phobically modified cationic peptide containing a long alkyl chain, for use in cancer-specific gene delivery. The cationic peptide is a substrate of protein kinase Cα (PKCα), which is known to be activated specifically in cancer cells. The hydrophobically modified LPEI-peptide conjugate (LPEI-C10-peptide) could form a polyplex with DNA through electrostatic and hydrophobic interactions between the anionic DNA strands and the cationic peptide substrate. The hydrophobic modification of the peptide did not affect the reactivity of the peptide toward PKCα, while the polyplex showed improved intracellular uptake. Because of the efficient endosomal escape and enhanced stability, the polyplex significantly improved the transgene regulation responding to intracellular PKCα activity.
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U2 - 10.1016/j.jconrel.2013.06.011
DO - 10.1016/j.jconrel.2013.06.011
M3 - Article
C2 - 23791979
AN - SCOPUS:84885096635
VL - 170
SP - 469
EP - 476
JO - Journal of Controlled Release
JF - Journal of Controlled Release
SN - 0168-3659
IS - 3
ER -
