Abstract
The amphiphilic α-helical peptide, Td3717, is a bi-functional synthetic peptide that acts as both a polycation for DNA binding and a ligand for targeted delivery to tumor cells. Td3717 forms a stable complex with plasmid DNA, and the complex maintained high transfection efficiency after storage at 4 °C for six months and after four freeze/thaw cycles. During the storage and freeze/thaw cycling, the particle size of the DNA/Td3717 complex remained less than 100 nm. The size of the complex is an important factor for its internalization into cells via the endocytosis pathway; therefore, the stability of the particles will strongly contribute to high transfection efficiencies after storage and repeated freezing/thawing.
| Original language | English |
|---|---|
| Pages (from-to) | 7643-7646 |
| Number of pages | 4 |
| Journal | Bioorganic and Medicinal Chemistry |
| Volume | 17 |
| Issue number | 22 |
| DOIs | |
| Publication status | Published - Nov 15 2009 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Pharmaceutical Science
- Drug Discovery
- Clinical Biochemistry
- Organic Chemistry
Cite this
Stability of DNA/Td3717 complexes for gene transfection, defined by the size and polydispersity of the complex. / Kuriyama, Shinichi; Taguchi, Yasushi; Watanabe, Kazuto; Nishimura, Kanako; Yanagibashi, Kazutoshi; Katayama, Yoshiki; Niidome, Takuro.
In: Bioorganic and Medicinal Chemistry, Vol. 17, No. 22, 15.11.2009, p. 7643-7646.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Stability of DNA/Td3717 complexes for gene transfection, defined by the size and polydispersity of the complex
AU - Kuriyama, Shinichi
AU - Taguchi, Yasushi
AU - Watanabe, Kazuto
AU - Nishimura, Kanako
AU - Yanagibashi, Kazutoshi
AU - Katayama, Yoshiki
AU - Niidome, Takuro
PY - 2009/11/15
Y1 - 2009/11/15
N2 - The amphiphilic α-helical peptide, Td3717, is a bi-functional synthetic peptide that acts as both a polycation for DNA binding and a ligand for targeted delivery to tumor cells. Td3717 forms a stable complex with plasmid DNA, and the complex maintained high transfection efficiency after storage at 4 °C for six months and after four freeze/thaw cycles. During the storage and freeze/thaw cycling, the particle size of the DNA/Td3717 complex remained less than 100 nm. The size of the complex is an important factor for its internalization into cells via the endocytosis pathway; therefore, the stability of the particles will strongly contribute to high transfection efficiencies after storage and repeated freezing/thawing.
AB - The amphiphilic α-helical peptide, Td3717, is a bi-functional synthetic peptide that acts as both a polycation for DNA binding and a ligand for targeted delivery to tumor cells. Td3717 forms a stable complex with plasmid DNA, and the complex maintained high transfection efficiency after storage at 4 °C for six months and after four freeze/thaw cycles. During the storage and freeze/thaw cycling, the particle size of the DNA/Td3717 complex remained less than 100 nm. The size of the complex is an important factor for its internalization into cells via the endocytosis pathway; therefore, the stability of the particles will strongly contribute to high transfection efficiencies after storage and repeated freezing/thawing.
UR - http://www.scopus.com/inward/record.url?scp=71749084071&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=71749084071&partnerID=8YFLogxK
U2 - 10.1016/j.bmc.2009.09.049
DO - 10.1016/j.bmc.2009.09.049
M3 - Article
C2 - 19836962
AN - SCOPUS:71749084071
VL - 17
SP - 7643
EP - 7646
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
SN - 0968-0896
IS - 22
ER -