聚(n-丙烯氨基酸)在水中介质的醣类相互作用.doc

聚(n-丙烯氨基酸)在水中介质的醣类相互作用.doc

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聚(n-丙烯氨基酸)在水中介质的醣类相互作用

功能性高分子期末報告 題目: Interaction of poly(N-acryloyl-amino acids) with saccharides in aqueous media Akihito Hashidzume, Atsushi Tanaka, Takahiro Sato Department of Macromolecular Science, Graduate School of Science, Osaka University, 1-1 Machikaneyama-cho, Toyonaka, Osaka 560-0043, Japan 姓名:宋昱杰 學號班級:化材四甲 abstract The interaction of a series of poly(N-acryloyl-amino acids) (pAXaa) with saccharides has been investigated by 1H NMR. 1H NMR for methyl-b-D-galactopyranoside (MbGal) in the presence of pAXaa indicatedthat hydrophobic interaction or hydrogen bonding was not considerable in the interaction of the polymerswith MbGal in aqueous media whereas CH?p interaction was relatively important. 1H NMR for several saccharides in the presence of poly(N-acryloyltryptophan) (pATrp) indicated that pATrp interactedmore strongly with the b-anomers than with the a-anomers presumably because of the triple CH?p interactions of the three axial protons in the b-anomers. In the interaction of pATrp with MbGal, MbGalinteracted with two or more Trp residues because Trp residues were localized on the polymer chain. 內容摘要 經 1H NMR一系列聚(的N -丙烯酰氨基酸)(pAXaa)與醣類相互作用已展開研究。pAXaa存在甲基- BD-半乳糖苷的1H NMR(MbGal)表示沒有相當的聚合物的相互作用,疏水相互作用或氫鍵MbGal在水介質中,而CH- P的相互作用是比較重要的。 1H核磁共振聚(N - acryloyltryptophan)(pATrp)存在的一些醣類表示pATrp互動更強烈,比anomers A - B - anomers大概是因為三聯的CH-在B- anomers三個軸向質子 p相互作用。在MbGal,MbGal pATrp與互動因為本地化的高分子鏈上的Trp殘基與兩個或兩個以上的Trp殘基相互作用。 Introduction Saccharides are one of important classes of compounds in biological systems, not only because saccharides are the energy source of living organisms but also because saccharides are the recognition sites on peptides, cells, and viruses [1,2]. In biological systems, saccharides interact with proteins, i.e., enzymes, antibodies, and lectins, to form complexes, resulting in expression of various functions [1,2]. Detail studies on binding sites for saccharides have indicated that complexes of saccharides with proteins are formed via hydrogen bonding, hydrophob

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