| Summary: | 碩士 === 台北醫學院 === 醫學研究所 === 90 === The most frequent genetic causes of amylotrophic scelosis (ALS) determined so far are mutations occurring in the gene coding for copper/znic superoxide dismutase (Cu,Zn-SOD). The mechanism may involve the formation of hydroxyl radicals or malfunctioning of the SOD
protein .
The development of peptide drugs and therapeutic proteins is limited
by the pool permeability and the selectivity of the cell membrane. A series of small protein domains , termed protein transduction domains
(PTDs) , have been shown to cross biological membranes efficiently and independently of specific transporters and receptors , and to promote the delivery of peptides and proteins into cells.
The human immunodeficiency virus type 1 (HIV-1) Tat protein
transduction domain (PTD), which posses a characteristic positive charge
on the basis of their enrichment of arginine and lysine residues activates transcription by specifically binding a stem-loop element in the viral long terminal repeat and is responsible for highly efficient protein transduction
through the plasma membrane.
Denatured Tat-SOD1 fusion protein was observed to successfully
transduced into undifferentiated PC12 cells and retained its activity via protein refolding.
It had been demonstracted that intraperitoneal injection of Tat-β
-galactosidase fusion protein resulted in delivery of the biologically
active fusion protein to all tissues in mice, including the brain (Dowdy, 1999).
According to it, we also purify the Tat-SOD1 fusion protein and want to observe that Tat-SOD1 fusion protein also can delivery efficiently to all tissue in mice by intraperitoneal injection.
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