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PEG-Poly(fumaric-sebacic acids)-PEG 삼중 블록 공중합체로 수용액에서 만들어진 폴리머솜의 분석과 방출특성
Pounehs. Pourhosseini,Ali A Saboury,Farhood Najafi,Adeleh Divsalar,Mohammad N Sarbolouki 한국고분자학회 2013 폴리머 Vol.37 No.3
Polymersomes made of biodegradable triblock copolymers based on poly(fumaric acid-co-sebacoyl chloride)/ PEG (PEG-co-P(FA/SC)-co-PEG) were prepared and studied in aqueous solutions. TEM confirmed the formation of vesicles in aqueous media. Aggregation behavior of the copolymers was studied by fluorescence spectroscopy of 8-anilino- 1-naphthalenesulfonic acid, and the critical aggregation concentration (c.a.c.) of the copolymer was found to be ~26.2 μM indicating desirable stability of the vesicles. Dynamic light scattering revealed that the size of the vesicles was distributed within the range of 170-270 nm. Turbidity measurements confirmed the relative short-term stability of the polymersomes. Carboxyfluorescein, a hydrophilic compound, was simply encapsulated in the vesicles during polymersome preparation. The release of encapsulant from the polymersomes at 25 and 37 oC lasted about 3 weeks, and the rate of release followed a first-order kinetics. The release is speculated to be primarily carried out through diffusion. These results confirm that these polymersomes are promising as controlled-release carriers of various drugs.
Nikkhah, Maryam,Naderi-Manesh, Hossein,Taghdir, Majid,Talebzadeh, Mehdi,Sadeghi-Zadeh, Majid,Schaller, Janatan,Sarbolouki, Mohamad N. Korean Society for Biochemistry and Molecular Biol 2006 Journal of biochemistry and molecular biology Vol.39 No.3
In this study, the cDNA of a new peptide from the venom of the scorpion, Buthotus saulcyi, was cloned and sequenced. It codes for a 64 residues peptide (Bsaul1) which shares high sequence similarity with depressant insect toxins of scorpions. The differences between them mainly appear in the loop1 which connects the $\beta$-strand1 to the $\alpha$-helix and seems to be functionally important in long chain scorpion neurotoxins. This loop is three amino acids longer in Bsaul1 compared to other depressant toxins. A comparative amino acid sequence analysis done on Bsaul1 and some of $\alpha$-, $\beta$-, excitatory and depressant toxins of scorpions showed that Bsaul1 contains all the residues which are highly conserved among long chain scorpion neurotoxins. Structural model of Bsaul1 was generated using Ts1 (a $\beta$-toxin that competes with the depressant insect toxins for binding to $Na^+$ channels) as template. According to the molecular model of Bsaul1, the folding of the polypeptide chain is being composed of an anti-parallel three-stranded $\beta$-sheet and a stretch of $\alpha$-helix, tightly bound by a set of four disulfide bridges. A striking similarity in the spatial arrangement of some critical residues was shown by superposition of the backbone conformation of Bsaul1 and Ts1.