Preparation and Function of Poly(acrylic acid)s Modified by Supramolecular Complex Composed of Porphinatoiron and a Cyclodextrin Dimer That Bind Diatomic Molecules (O2 and CO) in Aqueous Solution
Preparation and Function of Poly(acrylic acid)s Modified by Supramolecular Complex Composed of Porphinatoiron and a Cyclodextrin Dimer That Bind Diatomic Molecules (O2 and CO) in Aqueous Solution
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DOI：
10.1002/asia.201100354
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发表时间：
2011-11-04
影响因子：
4.1
通讯作者：
Kitagishi, Hiroaki
中科院分区：
文献类型：
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作者：
Kano, Koji;Ochi, Toshiro;Kitagishi, Hiroaki
用5-（4-β-丙氨酰氨基苯基）-10，15，20-三（4-磺酸基苯基）卟啉铁（III）对聚丙烯酸（PAA）进行改性，通过缩合反应得到含铁卟啉的PAA（FeP（n）s）。FeP（n）进一步通过Py 3CD官能化，Py 3CD是具有吡啶接头的全-O-甲基化β-环糊精（CD）二聚体，并且包括卟啉侧基以形成铁hemoCD-P（n）。在聚合物链中具有三个卟啉发色团的亚铁hemoCD-P（3）显示在pH 7.0和25 ℃的水溶液中结合分子氧（P-1/2 = 7.9 +/- 1.4托），得到氧-hemoCD-P（3）。氧合血红素CD-P（3）被双相自动氧化为铁血红素CD-P（3），其中27%的双氧加合物被快速氧化。在聚合物链中具有15个卟啉发色团的oxy-hemoCD-P（15）的自氧化速率比oxy-hemoCD-P（3）快得多，因此表明oxy-hemoCD-P（n）的自催化自氧化。过氧化氢酶可显著稳定氧合血红素CD-P（n），从而表明氧合血红素CD-P（n）产生的过氧化氢可加速自氧化。大部分注入大鼠股静脉的hemoCD-P（3）分子仍留在体内，但约有16%的hemoCD-P（3）分子以一氧化碳加合物的形式从尿液中排出。
Poly(acrylic acid) (PAA) is modified by 5-(4-beta-alanylaminophenyl)-10,15,20-tris(4-sulfonatophenyl) porphinatoiron(III) to yield iron porphyrin-bearing PAAs (FeP(n)s) through a condensation reaction. FeP(n)s were further functionalized by Py3CD, which is a per-O-methylated beta-cyclodextrin (CD) dimer with a pyridine linker and includes the porphyrin pendants to form ferric hemoCD-P(n) s. Ferrous hemoCD-P(3), having three porphyrin chromophores in a polymer chain, is shown to bind molecular oxygen (P-1/2 = 7.9 +/- 1.4 Torr) in aqueous solution at pH 7.0 and 25 degrees C, affording oxy-hemoCD-P(3). Oxy-hemoCD-P(3) is biphasically autoxidized to ferric hemoCD-P(3), with 27% of the dioxygen adducts being rapidly oxidized. The rate of autoxidation of oxy-hemoCD-P(15), having 15 porphyrin chromophores in a polymer chain, was much faster than that of oxy-hemoCD-P(3), thus suggesting self-catalyzed autoxidation of oxy-hemoCD-P(n)s. Oxy-hemoCD-P(n)s are markedly stabilized by catalase, thereby indicating that hydrogen peroxide generated from oxy-hemoCD-P(n) accelerates the autoxidation. Most of the hemoCD-P(3) molecules injected into the femoral vein of a rat remained in the body, though about 16% of the hemoCD-P(3) molecules were excreted in the urine as a carbon monoxide adduct.