高分子链在界面上的构象行为
摘要
在本论文中，我们主要利用带有耗散因子的石英晶体微天平(QCM-D)和Langmuir天平(LB)等手段对几种聚合物链在固／液及气／液界面上的构象行为进行了研究。首先，利用QCM-D对高分子刷的构象转变、聚合物链在固体表面的接枝动力学，以及聚电解质链的“层叠层”(layer-by-layer)自组装过程进行了系统研究。其次，我们利用LB对两种热敏性聚合物链在空气／水界面上的构象变化及其热敏性进行了探讨。最后，我们详细研究了PEO和OEO链在空气／水界面上的蛋白质阻抗机理。主要结果如下：
1．利用QCM-D对表面接枝的PNIPAM高分子刷在温度诱导下的塌缩-溶胀(collapse-swelling)过程进行了研究。在20℃到38℃的范围内，频率和耗散因子随着温度的升高逐渐地变化，表明了PNIPAM高分子刷是随着温度的升高而逐渐塌缩的，这与溶液中自由的PNIPAM链的相变过程迥异。我们认为固体表面对PNIPAM链的束缚作用、高分子刷的不均匀性以及链塌缩与脱水化间(dehydration)的协同性(cooperativity)都有可能导致这种高分子刷的连续相变。我们还研究了水—甲醇混合溶剂诱导的PNIPAM高分子刷的构象转变。水和甲醇都是PNIPAM的良溶剂，但水与甲醇在一定的比例下形成的络合物(complex)则是PNIPAM链的不良溶剂，因而随着混合溶剂中甲醇摩尔百分数的增加PNIPAM高分子刷经历了“溶胀—塌缩—溶胀”的转变过程。
2．利用QCM-D对端基为巯基的PNIPAM(HS-PNIPAM)链和PDEM(HS-PDEM)链在金表面接枝过程中的构象转变进行了研究。结果表明，链节间(segment-segment)以及链节与表面间(segment-surface)相互作用的竞争对于高分子刷的形成至关重要。对于短的HS-PNIPAM链而言，链节间的排斥相互作用以及链的弹性占主导作用，因而PNIPAM链的接枝过程表现出pancake-to-mushroom-to-brush的三阶段转变动力学过程。对于长的HS-PNIPAM链，链节和表面间的相互作用占主导作用，因而只会形成pancake结构，而不发生pancake-to-mushroom或pancake-to-brush的构象转变。在HS-PDEM体系中，我们也发现了三阶段接枝动力学过程，但由于HS-PDEM链与表面间作用很弱，并不发生pancake-to-mushroom的构象转变，只是从无规的mushroom构象调整为更加规整的mushroom构象，然后发生mushroom-to-brush的构象转变。
3．利用QCM-D研究了温度、pH以及盐的浓度对聚电解质链“层叠层”组装的影响。结果表明：(a)聚电解质多层膜的厚度随着温度的升高而逐渐增加。这主要是因为温度的升高加剧了相邻层间的相互渗透，从而有更多层高分子组装进去。温度升高所引起的憎水相互作用增强只对底部几层的组装起促进作用。(b)对于PSSS／PDEM体系，从pH=4增加到7，频率和耗散因子“振荡”中振幅增加，表明层与层间的渗透性增加，从而导致多层膜厚度增加。(c)聚电解质多层膜的厚度随着NaCl的浓度升高而增加。在低盐浓度时，PSSS／PVBTMAC的组装是由表面电荷反转水平控制的。在高盐浓度时，PSSS／PVBTMAC的组装则是电荷渗透深度决定。
4．利用LB对两种热敏性聚合物PNIPAM和PDEM在空气／水界面上的构象变化及热敏性进行了研究。(a)对于PNIPAM，当链在空气／水界面上呈现loops和tails构象时，由于PNIPAM链能顺利实现水化(去水化)，因而表现出明显的热敏性。此外，该构象态也表现出一定的压缩速率依赖性。当PNIPAM链在空气／水界面上呈现trains构象时，因为几乎所有的PNIPAM链节都吸附在界面上，温度和压缩速率对构象变化没有明显的影响。(b)对于PDEM，链的热敏性与其链上叔胺基团的水化(去水化)密切相关。综合分析可知：热敏性聚合物的相转变可能是由链的协同水化(去水化)引起的，且聚合物链在空气／水界面上的相转变行为与溶液中的迥然不同。
5．利用LB技术研究了蛋白质在PS_(108)-b-PEO_(114)和C_(16)H_(33)(OCH_2CH_2)_(10)OH覆盖的空气／水界面上的吸附。蛋白质在PS_(108)-b-PEO_(114)覆盖的空气／水界面上吸附时，在特定的排列密度(σ)处(σ~(-1)=10nm~2)存在一个吸附量的极低值。这主要是由于在σ~(-1)＞10nm~2的范围内，PEO链仅仅起立体位阻作用，即PEO的蛋白质阻抗能力随着σ的增加而增强。在σ~(-1)＜10nm~2的范围内，蛋白质和PEO链间的粘附作用占据主导作用。随着σ的增加，表面压升高，即蛋白质阻抗能力随着σ的增加逐渐减弱。对于C_(16)H_(33)(OCH_2CH_2)_(10)OH覆盖的空气／水界面，蛋白质的吸附量始终随着σ的增加而减小，说明其蛋白质阻抗能力随着σ的增加逐渐增强。这是由于在整个排列密度范围内OEO链仅仅起立体位阻效应造成的。另一方面，在蛋白质的吸附动力学过程中，纤维蛋白原的吸附过程表现出三个不同的过程，即“扩散—渗透—重排”过程；而溶菌酶的吸附只观察到后面两个过程，这可能是由于后者在溶液中具有较大的扩散系数所导致的。
This thesis deals with the conformational change of polymer chains at the solid/liquid or air/water interfaces. First, we have investigated the conformation transition of polymer brush and the kinetics of formation of polymer brush at the solid surface, and the self-assembly of polyelectrolyte layer-by-layer deposition. Second, we have studied the conformation and thermosensitivity of the polymers at the air/water interface. Third, we have investigated the mechanism of protein resistance of poly(ethylene oxide) (PEO) and oligo(ethylene oxide) (OEO) chains at the air/water interface. The main results are as follows:
1. The temperature induced collapse-to-swelling transition of poly(N-isopropylacrylamide) (PNIPAM) brush grafted on oscillator surface was investigated by using quartz crystal microbalance with dissipation (QCM-D). In the range of 20°C to 38°C, frequency and dissipation gradually change with temperature, indicating that PNIPAM brush gradually collapses. This is in contrast to free PNIPAM chains in solution, which exhibit a sharp collapse transition. The surface restriction, the non-uniformity of polymer brush and the cooperativity between collapse and dehydration transition are thought to be responsible for such a continuous collapse. We have also studied the conformational change of PNIPAM brush in water-methanol mixture. PNIPAM chains swell in either water or methanol. However, as the molar fraction of methanol increases, PNIPAM brush undergoes a swelling-to-collapse-to-swelling transition. The collapse of PNIPAM brush is attributed to the formation of water-methanol complexes which are poor solvents for PNIPAM chains.
2. The kinetics of formation of polymer brush of thiol-terminated poly(N-isopropylacrylamide) (HS-PNIPAM) and thiol-terminated poly[(2-dimethylamino)ethyl methacrylate] (HS-PDEM) chains on a gold-coated oscillator surface was investigated by use of QCM-D. In the case of HS-PNIPAM, the frequency and energy dissipation responses revealed that short HS-PNIPAM chains exhibit a three-regime-kinetics of the grafting. In regime I and II, the HS-PNIPAM chains form a pancake and mushroom structure, respectively. In regime III, the chains form brushes. From regime II to regime III, the mushroom-to-brush transition occurs. For the longer HS-PNIPAM chains, due to the strong segment-surface interaction, the segments cannot desorb from the surface, so the chains do not undergo a pancake-to-brush transition. In the case of HS-PDEM, the frequency and energy dissipation responses also reveal a three-regime-kinetics of the grafting. The chains are quickly grafted in regime I forming a random mushroom. In regime II, the grafted chains have a rearrangement to form an ordered mushroom structure. The grafting is accelerated in regime III. As the grafting density increases, the chains form brushes. From regime II to regime III, the mushroom-to-brush transition occurs.
3. The effects of temperature, pH and salt concentration on layer-by-layer deposition of polyelectrolyte chains have also been investigated by use of QCM-D. The investigations lead to the following conclusions: (a) The thickness of polyelectrolyte mutilayers increases with temperature. This is because the increasing temperature leads to the increase of penetration between neighboring layers. The hydrophobic effect induced by temperature only facilitates the deposition in the initial several layers. (b) In the case of PSSS/PDEM, from pH = 4 to 7, the amplitudes of oscillation in frequency and dissipation increase with pH, indicating that the increase of penetration between layers, which leads to a thicker film. (c) The thickness of polyelectrolyte mutilayers increases with the concentration of NaCl. In the low salt concentration regime, the deposition of PSSS/PVBTMAC is dominated by the level of surface charge overcompensation. In contrast, in the high salt concentration regime, the deposition is dominated by charge penetration length.
4. The conformation and thermosensitivty of two polymers at the air/water interface have been studied by use of Langmuir balance. (a) In the case of PNIPAM, when loops or tails are formed at the interface, PNIPAM chains exhibit thermosensitive properties due to hydration (dehydration) depending on the compression rate. When PNIPAM chains take train conformation at the air/water interface, however, the surface pressure changes are nearly independent of temperature and compression rate because almost all segments of the PNIPAM chains are adsorbed at the interface. (b) In the case of PDEM, it shows the thermosensitivity relates to the hydration (dehydration) of the tertiary amine group. Our results demonstrate that the phase transition of the thermosensitive polymers is probably started by the cooperative hydration (dehydration) and the phase transition at the air/water interface is markedly different from that in aqueous solution.
5. Protein adsorption on polystyrene-block-poly(ethylene oxide) (PS_(108)-b-PEO_(114)) and C_(16)H_(33)(OCH_2CH_2)_(10)OH monolayers was studied by using the Langmuir technique. In the case of PEO monolayer, a protein adsorption minimum is clearly revealed at σ~(-1) = 10 nm~2 for both lysozyme and fibrinogen. Manifested are two grafting density regimes of steric repulsion and compressive attraction between PEO and protein on top of the overall attraction of protein to the air/water interface. The observed protein adsorption minimum coincides with the maximum of the surface segment density at σ~(-1) = 10 nm~2. However, OEO monolayer presents a different scenario, namely, the amount of protein adsorbed decreases monotonically with increasing grafting density, indicating that the OEO chains merely act as steric barrier to protein adsorption onto the air/water interface. In the adsorption of fibrinogen, three distinct kinetic regimes controlled by diffusion, penetration and rearrangement are recognized, whereas only the latter two are made out in the adsorption of lysozyme. This can be ascribed to the relatively larger diffusion coefficient of lysozyme.
1．利用QCM-D对表面接枝的PNIPAM高分子刷在温度诱导下的塌缩-溶胀(collapse-swelling)过程进行了研究。在20℃到38℃的范围内，频率和耗散因子随着温度的升高逐渐地变化，表明了PNIPAM高分子刷是随着温度的升高而逐渐塌缩的，这与溶液中自由的PNIPAM链的相变过程迥异。我们认为固体表面对PNIPAM链的束缚作用、高分子刷的不均匀性以及链塌缩与脱水化间(dehydration)的协同性(cooperativity)都有可能导致这种高分子刷的连续相变。我们还研究了水—甲醇混合溶剂诱导的PNIPAM高分子刷的构象转变。水和甲醇都是PNIPAM的良溶剂，但水与甲醇在一定的比例下形成的络合物(complex)则是PNIPAM链的不良溶剂，因而随着混合溶剂中甲醇摩尔百分数的增加PNIPAM高分子刷经历了“溶胀—塌缩—溶胀”的转变过程。
2．利用QCM-D对端基为巯基的PNIPAM(HS-PNIPAM)链和PDEM(HS-PDEM)链在金表面接枝过程中的构象转变进行了研究。结果表明，链节间(segment-segment)以及链节与表面间(segment-surface)相互作用的竞争对于高分子刷的形成至关重要。对于短的HS-PNIPAM链而言，链节间的排斥相互作用以及链的弹性占主导作用，因而PNIPAM链的接枝过程表现出pancake-to-mushroom-to-brush的三阶段转变动力学过程。对于长的HS-PNIPAM链，链节和表面间的相互作用占主导作用，因而只会形成pancake结构，而不发生pancake-to-mushroom或pancake-to-brush的构象转变。在HS-PDEM体系中，我们也发现了三阶段接枝动力学过程，但由于HS-PDEM链与表面间作用很弱，并不发生pancake-to-mushroom的构象转变，只是从无规的mushroom构象调整为更加规整的mushroom构象，然后发生mushroom-to-brush的构象转变。
3．利用QCM-D研究了温度、pH以及盐的浓度对聚电解质链“层叠层”组装的影响。结果表明：(a)聚电解质多层膜的厚度随着温度的升高而逐渐增加。这主要是因为温度的升高加剧了相邻层间的相互渗透，从而有更多层高分子组装进去。温度升高所引起的憎水相互作用增强只对底部几层的组装起促进作用。(b)对于PSSS／PDEM体系，从pH=4增加到7，频率和耗散因子“振荡”中振幅增加，表明层与层间的渗透性增加，从而导致多层膜厚度增加。(c)聚电解质多层膜的厚度随着NaCl的浓度升高而增加。在低盐浓度时，PSSS／PVBTMAC的组装是由表面电荷反转水平控制的。在高盐浓度时，PSSS／PVBTMAC的组装则是电荷渗透深度决定。
4．利用LB对两种热敏性聚合物PNIPAM和PDEM在空气／水界面上的构象变化及热敏性进行了研究。(a)对于PNIPAM，当链在空气／水界面上呈现loops和tails构象时，由于PNIPAM链能顺利实现水化(去水化)，因而表现出明显的热敏性。此外，该构象态也表现出一定的压缩速率依赖性。当PNIPAM链在空气／水界面上呈现trains构象时，因为几乎所有的PNIPAM链节都吸附在界面上，温度和压缩速率对构象变化没有明显的影响。(b)对于PDEM，链的热敏性与其链上叔胺基团的水化(去水化)密切相关。综合分析可知：热敏性聚合物的相转变可能是由链的协同水化(去水化)引起的，且聚合物链在空气／水界面上的相转变行为与溶液中的迥然不同。
5．利用LB技术研究了蛋白质在PS_(108)-b-PEO_(114)和C_(16)H_(33)(OCH_2CH_2)_(10)OH覆盖的空气／水界面上的吸附。蛋白质在PS_(108)-b-PEO_(114)覆盖的空气／水界面上吸附时，在特定的排列密度(σ)处(σ~(-1)=10nm~2)存在一个吸附量的极低值。这主要是由于在σ~(-1)＞10nm~2的范围内，PEO链仅仅起立体位阻作用，即PEO的蛋白质阻抗能力随着σ的增加而增强。在σ~(-1)＜10nm~2的范围内，蛋白质和PEO链间的粘附作用占据主导作用。随着σ的增加，表面压升高，即蛋白质阻抗能力随着σ的增加逐渐减弱。对于C_(16)H_(33)(OCH_2CH_2)_(10)OH覆盖的空气／水界面，蛋白质的吸附量始终随着σ的增加而减小，说明其蛋白质阻抗能力随着σ的增加逐渐增强。这是由于在整个排列密度范围内OEO链仅仅起立体位阻效应造成的。另一方面，在蛋白质的吸附动力学过程中，纤维蛋白原的吸附过程表现出三个不同的过程，即“扩散—渗透—重排”过程；而溶菌酶的吸附只观察到后面两个过程，这可能是由于后者在溶液中具有较大的扩散系数所导致的。
This thesis deals with the conformational change of polymer chains at the solid/liquid or air/water interfaces. First, we have investigated the conformation transition of polymer brush and the kinetics of formation of polymer brush at the solid surface, and the self-assembly of polyelectrolyte layer-by-layer deposition. Second, we have studied the conformation and thermosensitivity of the polymers at the air/water interface. Third, we have investigated the mechanism of protein resistance of poly(ethylene oxide) (PEO) and oligo(ethylene oxide) (OEO) chains at the air/water interface. The main results are as follows:
1. The temperature induced collapse-to-swelling transition of poly(N-isopropylacrylamide) (PNIPAM) brush grafted on oscillator surface was investigated by using quartz crystal microbalance with dissipation (QCM-D). In the range of 20°C to 38°C, frequency and dissipation gradually change with temperature, indicating that PNIPAM brush gradually collapses. This is in contrast to free PNIPAM chains in solution, which exhibit a sharp collapse transition. The surface restriction, the non-uniformity of polymer brush and the cooperativity between collapse and dehydration transition are thought to be responsible for such a continuous collapse. We have also studied the conformational change of PNIPAM brush in water-methanol mixture. PNIPAM chains swell in either water or methanol. However, as the molar fraction of methanol increases, PNIPAM brush undergoes a swelling-to-collapse-to-swelling transition. The collapse of PNIPAM brush is attributed to the formation of water-methanol complexes which are poor solvents for PNIPAM chains.
2. The kinetics of formation of polymer brush of thiol-terminated poly(N-isopropylacrylamide) (HS-PNIPAM) and thiol-terminated poly[(2-dimethylamino)ethyl methacrylate] (HS-PDEM) chains on a gold-coated oscillator surface was investigated by use of QCM-D. In the case of HS-PNIPAM, the frequency and energy dissipation responses revealed that short HS-PNIPAM chains exhibit a three-regime-kinetics of the grafting. In regime I and II, the HS-PNIPAM chains form a pancake and mushroom structure, respectively. In regime III, the chains form brushes. From regime II to regime III, the mushroom-to-brush transition occurs. For the longer HS-PNIPAM chains, due to the strong segment-surface interaction, the segments cannot desorb from the surface, so the chains do not undergo a pancake-to-brush transition. In the case of HS-PDEM, the frequency and energy dissipation responses also reveal a three-regime-kinetics of the grafting. The chains are quickly grafted in regime I forming a random mushroom. In regime II, the grafted chains have a rearrangement to form an ordered mushroom structure. The grafting is accelerated in regime III. As the grafting density increases, the chains form brushes. From regime II to regime III, the mushroom-to-brush transition occurs.
3. The effects of temperature, pH and salt concentration on layer-by-layer deposition of polyelectrolyte chains have also been investigated by use of QCM-D. The investigations lead to the following conclusions: (a) The thickness of polyelectrolyte mutilayers increases with temperature. This is because the increasing temperature leads to the increase of penetration between neighboring layers. The hydrophobic effect induced by temperature only facilitates the deposition in the initial several layers. (b) In the case of PSSS/PDEM, from pH = 4 to 7, the amplitudes of oscillation in frequency and dissipation increase with pH, indicating that the increase of penetration between layers, which leads to a thicker film. (c) The thickness of polyelectrolyte mutilayers increases with the concentration of NaCl. In the low salt concentration regime, the deposition of PSSS/PVBTMAC is dominated by the level of surface charge overcompensation. In contrast, in the high salt concentration regime, the deposition is dominated by charge penetration length.
4. The conformation and thermosensitivty of two polymers at the air/water interface have been studied by use of Langmuir balance. (a) In the case of PNIPAM, when loops or tails are formed at the interface, PNIPAM chains exhibit thermosensitive properties due to hydration (dehydration) depending on the compression rate. When PNIPAM chains take train conformation at the air/water interface, however, the surface pressure changes are nearly independent of temperature and compression rate because almost all segments of the PNIPAM chains are adsorbed at the interface. (b) In the case of PDEM, it shows the thermosensitivity relates to the hydration (dehydration) of the tertiary amine group. Our results demonstrate that the phase transition of the thermosensitive polymers is probably started by the cooperative hydration (dehydration) and the phase transition at the air/water interface is markedly different from that in aqueous solution.
5. Protein adsorption on polystyrene-block-poly(ethylene oxide) (PS_(108)-b-PEO_(114)) and C_(16)H_(33)(OCH_2CH_2)_(10)OH monolayers was studied by using the Langmuir technique. In the case of PEO monolayer, a protein adsorption minimum is clearly revealed at σ~(-1) = 10 nm~2 for both lysozyme and fibrinogen. Manifested are two grafting density regimes of steric repulsion and compressive attraction between PEO and protein on top of the overall attraction of protein to the air/water interface. The observed protein adsorption minimum coincides with the maximum of the surface segment density at σ~(-1) = 10 nm~2. However, OEO monolayer presents a different scenario, namely, the amount of protein adsorbed decreases monotonically with increasing grafting density, indicating that the OEO chains merely act as steric barrier to protein adsorption onto the air/water interface. In the adsorption of fibrinogen, three distinct kinetic regimes controlled by diffusion, penetration and rearrangement are recognized, whereas only the latter two are made out in the adsorption of lysozyme. This can be ascribed to the relatively larger diffusion coefficient of lysozyme.
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