蛋白质聚集的多酚抑制调控机制及其材料应用研究
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摘要
本论文以蛋白质聚集和淀粉样纤维化为研究对象，考察天然产物多酚对蛋白质聚集和淀粉样纤维化过程抑制作用，揭示调控机理，并探索蛋白质聚集及其淀粉样纤维在药物递送和功能材料领域的应用。
（1）多酚调控胰岛素聚集动力学研究：考察不同多酚化合物对胰岛素淀粉样聚集动力学和形貌结构的影响，研究多酚调控胰岛素聚集过程的作用机制。重点揭示原花青素作用机制为形成原花青素/胰岛素中间聚集体，抑制胰岛素聚集成核过程；分析得出多酚氧化还原性质、化学结构和蛋白质固有性质是影响多酚抑制聚集能力的关键因素。
（2）激光-芳香小分子解聚胰岛素淀粉样纤维机理研究：建立激光芳香小分子耦合法解聚胰岛素淀粉样纤维方法，利用稳瞬态荧光光谱、密度泛函理论和分子对接计算揭示激光-芳香小分子解聚作用机理以及芳香分子结构和解聚作用关系。研究结果表明激光-芳香小分子解聚本质是扰乱胰岛素淀粉样纤维之间疏水作用，解聚必要条件为小分子与胰岛素淀粉样纤维有效结合，并且激光照射下小分子激发态改变胰岛素淀粉样纤维周围疏水环境。
（3）原花青素-胰岛素长效纳米药物制备：以天然低聚原花青素（OPC）作为胰岛素聚集体交联剂和稳定剂，提出了一种可控稳定制备长效胰岛素纳米药物的方法。胰岛素聚集体尺寸由OPC浓度、pH值和聚集时间等因素调控，最优条件为100μM OPC、pH7PBS缓冲溶液和聚集时间6h；在该条件下OPC–胰岛素纳米颗粒37天仅释放~21%胰岛素，有望成为一种潜在的长效释放药物。
（4）β-乳球蛋白聚集法制备金纳米链药载茶多酚：利用热聚集法制备一种茶多酚（TPP）药载的AuNPs/β-LGA纳米链，聚集链长度由TPP浓度、聚集时间和溶液pH调控，最优条件为10μM TPP、聚集时间30min和PBS中性溶液，可形成3─5个AuNPs长度纳米链。该方法结合了β-LG对TPP分子抗氧化保护能力和AuNPs检测应用潜力，同时金纳米链也显示出ThT荧光响应信号。
（5）β-乳球蛋白聚集模板制备氧化石墨烯纤维及其薄膜性质：以β-LGA作为模板，利用静电和疏水作用制备一种β-LGA/GO纳米纤维及其薄膜材料，形貌结构由溶液pH值和GO/β-LGA体积比调控，最优条件为pH4.6和体积比30：1，可形成直径为20─50nm纳米纤维。结果表明β-LGA/GO薄膜具有较好的电容性质和亲水性，有望用于细胞培养领域。
The present work is concerned with protein aggration and amyloid fibrillation.We concentrate on studying the inhibition of natural polyphenols on protein amyloidfibrillation experimentally and theoretically, which can lead to a better understandingof the polyphenol-regulated mechanism during this process and to give a possiblegeneral mechanism. We try to explore the application of protein aggregation and itsproduct amyloid fibrils on protein drug delivery and material functionalization.
First of all, we focused on the effects of different polyphenol compounds on thekinetics of insulin aggregation, as well as the structure and morphology of insulinaggregates using various biophysical technologies. Oligomeric polyphenolcompounds showed potent inhibition at all stages of insulin fibrillation and redirectinsulin aggregation pathway via the formation of unstructured, off-pathwayaggregates. The results suggested that the antioxidative activity, chemical structure,and protein inherent properties were key factors on the anti-amyloidogenic activity ofpolyphenol.
Secondly, insulin amyloid fibrils were disaggregated by laser irradiation coupledwith small aromatic molecules. We investigated the inhibition mechanism by acombination of steady-state/time-resolved fluorescence spectroscopy, DFT calculation,and molecular docking. The results suggested that the nature of disaggregation was todisrupt hydrophobic interactions between insulin amyloid fibrils. Destruction ofamyloid fibrils would occur when small molecules could bind to insulin fibrilsefficiently and change the hydrophobic environment surrounding amyloid fibrils.
Thirdly, natural oligomeric procyanidin (OPC) with high pharmacological andbiological activities was successfully used to synthesize OPC–insulin (OPC–INS)nanoparticles with different aggregation sizes for sustained and controlled delivery ofhydrophilic insulin. The aggregation size of OPC–INS nanoparticles was regulated byOPC concentration, pH value, and incubation time. The optimal condition was thatinsulin incubated with100μM OPC for6h in pH7PBS buffer. In the self-assemblyof insulin, OPC could serve both in the encompassing of insulin aggregates as astabilizer and cross-linking different amounts of insulin aggregates into OPC–INS nanoparticles as interphase. In the best case for OPC–INS nanoparticles, only~21%of insulin was released in37d. This study showed that the OPC–INS nanosystem ispromising to serve as a long-acting insulin release formulation, and OPC has greatpotential as a drug carrier for nanomedicine.
Fourthly, we utilized the aggregation of β-LG to form β-LGA-coated AuNPsnanochains for drug delivery of tea polyphenol (TPP). The length ofAuNPs/β-LGA/TPP nanochains was regulated by TPP concentration, aggregationtime and pH value. The optimal condition was TPP of10μM in pH7PBS for30minof incubation time, under which condition we obtained AuNPs/β-LGA/TPP consisted3─5AuNPs. This nanochain could benefit from the protection effect of β-LGA onTPP antioxidant activity and the potential detection application of AuNPs.Furthermore, the nanochains have also shown ThT fluorescence response intensity.
Lastly, the β-LGA/GO nanofibrils and its thin film were prepared by usingβ-LGA amyloid fibrils as templates via electrostatic and hydrophobic interaction. Themorphology of β-LGA/GO nanofibrils was regulated by pH value and the volumeratio of GO to β-LGA. The optimal condition was pH4.6with the GO/β-LGA ratio of30:1, under which condition β-LGA/GO nanofibrils had a diameter of20─50nm. Theresults suggested that β-LGA/GO thin film has a better capacitance and hydrophilicproperties, facilitating its application in the filed of cell culture.
（1）多酚调控胰岛素聚集动力学研究：考察不同多酚化合物对胰岛素淀粉样聚集动力学和形貌结构的影响，研究多酚调控胰岛素聚集过程的作用机制。重点揭示原花青素作用机制为形成原花青素/胰岛素中间聚集体，抑制胰岛素聚集成核过程；分析得出多酚氧化还原性质、化学结构和蛋白质固有性质是影响多酚抑制聚集能力的关键因素。
（2）激光-芳香小分子解聚胰岛素淀粉样纤维机理研究：建立激光芳香小分子耦合法解聚胰岛素淀粉样纤维方法，利用稳瞬态荧光光谱、密度泛函理论和分子对接计算揭示激光-芳香小分子解聚作用机理以及芳香分子结构和解聚作用关系。研究结果表明激光-芳香小分子解聚本质是扰乱胰岛素淀粉样纤维之间疏水作用，解聚必要条件为小分子与胰岛素淀粉样纤维有效结合，并且激光照射下小分子激发态改变胰岛素淀粉样纤维周围疏水环境。
（3）原花青素-胰岛素长效纳米药物制备：以天然低聚原花青素（OPC）作为胰岛素聚集体交联剂和稳定剂，提出了一种可控稳定制备长效胰岛素纳米药物的方法。胰岛素聚集体尺寸由OPC浓度、pH值和聚集时间等因素调控，最优条件为100μM OPC、pH7PBS缓冲溶液和聚集时间6h；在该条件下OPC–胰岛素纳米颗粒37天仅释放~21%胰岛素，有望成为一种潜在的长效释放药物。
（4）β-乳球蛋白聚集法制备金纳米链药载茶多酚：利用热聚集法制备一种茶多酚（TPP）药载的AuNPs/β-LGA纳米链，聚集链长度由TPP浓度、聚集时间和溶液pH调控，最优条件为10μM TPP、聚集时间30min和PBS中性溶液，可形成3─5个AuNPs长度纳米链。该方法结合了β-LG对TPP分子抗氧化保护能力和AuNPs检测应用潜力，同时金纳米链也显示出ThT荧光响应信号。
（5）β-乳球蛋白聚集模板制备氧化石墨烯纤维及其薄膜性质：以β-LGA作为模板，利用静电和疏水作用制备一种β-LGA/GO纳米纤维及其薄膜材料，形貌结构由溶液pH值和GO/β-LGA体积比调控，最优条件为pH4.6和体积比30：1，可形成直径为20─50nm纳米纤维。结果表明β-LGA/GO薄膜具有较好的电容性质和亲水性，有望用于细胞培养领域。
The present work is concerned with protein aggration and amyloid fibrillation.We concentrate on studying the inhibition of natural polyphenols on protein amyloidfibrillation experimentally and theoretically, which can lead to a better understandingof the polyphenol-regulated mechanism during this process and to give a possiblegeneral mechanism. We try to explore the application of protein aggregation and itsproduct amyloid fibrils on protein drug delivery and material functionalization.
First of all, we focused on the effects of different polyphenol compounds on thekinetics of insulin aggregation, as well as the structure and morphology of insulinaggregates using various biophysical technologies. Oligomeric polyphenolcompounds showed potent inhibition at all stages of insulin fibrillation and redirectinsulin aggregation pathway via the formation of unstructured, off-pathwayaggregates. The results suggested that the antioxidative activity, chemical structure,and protein inherent properties were key factors on the anti-amyloidogenic activity ofpolyphenol.
Secondly, insulin amyloid fibrils were disaggregated by laser irradiation coupledwith small aromatic molecules. We investigated the inhibition mechanism by acombination of steady-state/time-resolved fluorescence spectroscopy, DFT calculation,and molecular docking. The results suggested that the nature of disaggregation was todisrupt hydrophobic interactions between insulin amyloid fibrils. Destruction ofamyloid fibrils would occur when small molecules could bind to insulin fibrilsefficiently and change the hydrophobic environment surrounding amyloid fibrils.
Thirdly, natural oligomeric procyanidin (OPC) with high pharmacological andbiological activities was successfully used to synthesize OPC–insulin (OPC–INS)nanoparticles with different aggregation sizes for sustained and controlled delivery ofhydrophilic insulin. The aggregation size of OPC–INS nanoparticles was regulated byOPC concentration, pH value, and incubation time. The optimal condition was thatinsulin incubated with100μM OPC for6h in pH7PBS buffer. In the self-assemblyof insulin, OPC could serve both in the encompassing of insulin aggregates as astabilizer and cross-linking different amounts of insulin aggregates into OPC–INS nanoparticles as interphase. In the best case for OPC–INS nanoparticles, only~21%of insulin was released in37d. This study showed that the OPC–INS nanosystem ispromising to serve as a long-acting insulin release formulation, and OPC has greatpotential as a drug carrier for nanomedicine.
Fourthly, we utilized the aggregation of β-LG to form β-LGA-coated AuNPsnanochains for drug delivery of tea polyphenol (TPP). The length ofAuNPs/β-LGA/TPP nanochains was regulated by TPP concentration, aggregationtime and pH value. The optimal condition was TPP of10μM in pH7PBS for30minof incubation time, under which condition we obtained AuNPs/β-LGA/TPP consisted3─5AuNPs. This nanochain could benefit from the protection effect of β-LGA onTPP antioxidant activity and the potential detection application of AuNPs.Furthermore, the nanochains have also shown ThT fluorescence response intensity.
Lastly, the β-LGA/GO nanofibrils and its thin film were prepared by usingβ-LGA amyloid fibrils as templates via electrostatic and hydrophobic interaction. Themorphology of β-LGA/GO nanofibrils was regulated by pH value and the volumeratio of GO to β-LGA. The optimal condition was pH4.6with the GO/β-LGA ratio of30:1, under which condition β-LGA/GO nanofibrils had a diameter of20─50nm. Theresults suggested that β-LGA/GO thin film has a better capacitance and hydrophilicproperties, facilitating its application in the filed of cell culture.
引文
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