DocumentCode :
3378440
Title :
Phosphorylatable short peptide for facilitating DNA transfection
Author :
Ma, Jingcai ; Cao, Xiaona ; Zhou, Shumin ; Kong, Fanqiang ; Ren, Yuping ; Zhao, Ronglan ; Liang, Dongchun ; Zhang, Jingyu
Author_Institution :
Inst. of Endocrinology/Metabolic Disease Hosp., Tianjin Med. Univ., Tianjin, China
fYear :
2009
fDate :
13-14 Dec. 2009
Firstpage :
461
Lastpage :
464
Abstract :
A phosphorylatable short peptide(pSP) with the amino acid composition of ¿LLLRRRDNEYFYVRRLL¿ containing two potentially phosphorylatable tyrosine residues was chemically synthesized. This short peptide was characteristic with the isoelectric point of 10.88 and could be positively charged under physiological condition. The ¿DNEYFYV¿ motif in the pSP is the substrate of Jak2 kinase which was verified of being constantly expressed in mammalian cells. Meanwhile another kind of nonphosphorylatable npSP of ¿LLLRRRDNEEFGVRRLL¿ was also synthesized as control. Either pSP or npSP was made into complex with plasmid DNA containing luciferase reporter gene. In vitro phosphorylation and DNA releasing assays demonstrated that cell lysate could phosphorylated the pSP and hence facilitated DNA unpacking from the complex. Thereafter C2C12 mouse myoblast cells were transfected by pSP/DNA and npSP/DNA complexes respectivly and the transfection efficiency was represented by lucifersace activity in the cell lysate.
Keywords :
DNA; biochemistry; cellular biophysics; molecular biophysics; C2C12 mouse myoblast cells; DNA transfection; Jak2 kinase; amino acid; isoelectric point; luciferase reporter gene; mammalian cells; phosphorylatable short peptide; tyrosine residue; Amino acids; Cells (biology); DNA; Hospitals; Immune system; In vitro; Mice; Peptides; Proteins; Temperature; kinase substrated; short peptide; transfection;
fLanguage :
English
Publisher :
ieee
Conference_Titel :
BioMedical Information Engineering, 2009. FBIE 2009. International Conference on Future
Conference_Location :
Sanya
Print_ISBN :
978-1-4244-4690-2
Electronic_ISBN :
978-1-4244-4692-6
Type :
conf
DOI :
10.1109/FBIE.2009.5405819
Filename :
5405819
Link To Document :
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