燕麦蛋白结构、自组装性质及其纳米纤维形成研究
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摘要
蛋白纳米纤维聚集的研究可以为人体中蛋白质纤维化自组装导致的帕金森、老年痴呆症等20多种疾病的治疗提供重要借鉴和启示;作为生物材料替生物工程和制药工程提供自组装载体,携带活性成分或药物;为饮料和火腿食品等高糖分和高脂肪的产品中取代多糖类成分和脂肪成分起到增稠作用和降低热量的同时,起到补充氨基酸配比合理、营养均衡蛋白质的作用;作为清水凝胶的促凝剂,起到降低凝胶成本的作用;课题的实施能对医学上蛋白自组装类疾病的治疗、制药工程、生物材料和保健食品的发展有积极的推动作用。
本论文以燕麦分离蛋白和燕麦球蛋白为原料,通过氨基酸分析仪、SDS-PAGE、红外光谱仪、园二色谱、敲击式原子力扫描电镜、透射电镜和动态流变仪、动态光散射等研究燕麦分离蛋白和燕麦球蛋白的氨基酸组成、二级结构和聚集等性质;采用原子力扫描电镜和透射电镜在纳米尺度下对影响其纳米纤维形成的理化因素进行比较,并运用多种手段对其纳米纤维的形貌和特性进行表征;通过进一步对燕麦分离蛋白进行分子修饰,达到提高其功能特性的目的,同时深入研究修饰对燕麦分离蛋白纳米纤维形成产生的影响,主要研究结果如下:
燕麦分离蛋白OPI的多肽分子量在14.0 kDa到66.0 kDa之间,谷氨酸和亮氨酸含量分别高达24.7%,8.1%;燕麦分离蛋白含有大约7%β-转曲, 19%α-螺旋,和74%β-折叠;敲击式原子力扫描电镜结果显示燕麦分离蛋白主要以两种形状存在,椭球形和碟盘形;在浓度低于0.5 mg/mL时,OPI分子以单个分子形式存在,当浓度高于1.0 mg/mL时,许多OPI分子相互聚集会形成颗粒大小分布不均匀的聚集体;燕麦球蛋白的多肽分子量在10.0 KDa to 70.0 Kda之间,谷氨酸和精氨酸含量分别高达24.2%和9.0%,红外光谱结果表面,燕麦球蛋白含有大约8.5%β-转曲, 10.2%α-螺旋, 81.3%β-折叠。原子力扫描显微镜结果表明燕麦球蛋白分子主要以椭球形式存在,在球蛋白分子浓度低于0.1 mg/mL时,球蛋白分子以单个分子形式存在,当浓度高于0.5 mg/mL时,球蛋白分子即自组装形成颗粒大小分布不均的聚集体;动态光散射结果表明球蛋白的平均水合半径大约为39.8nm,颗粒大小主要在6nm-200nm之间,其中,水合半径在6nm左右的颗粒数量占总数的90%以上,具有较大水合半径的是球蛋白自组装形成的聚集体,研究结果与原子力扫描电镜和透射电镜结果一致。
燕麦球蛋白分子能在85°C,蛋白浓度1~10 mg/ml, pH 2条件下,加热24小时的过程中形成直径12nm左右,长度0~10μm的纳米纤维,纳米纤维的平均长度与加热时间成正相关,而纤维直径基本保持一致,具有螺旋周期结构;纳米纤维形成过程中燕麦球蛋白分子二级结构和三级结构显著发生变化,同时伴随着多肽链的降解,在12小时后,体系中多肽的分子量降低到<20 kDa以下,β-折叠含量显著增加。
燕麦分离蛋白能在pH2,85°C,搅拌速度400rad/s条件下随着加热时间的延长形成长度0~7μm的纳米纤维,纳米纤维长度分布不均但直径基本相同,具有螺旋周期结构;体系中蛋白分子的水合半径Rh随着加热时间延期逐渐增加;燕麦球蛋白与燕麦分离蛋白的不同之处在于燕麦球蛋白在搅拌速度为0rad/s的情况下也能形成纳米纤维,燕麦球蛋白在同样条件下,纤维的平均长度更长,颗粒形成纤维的转化率更高,纤维的螺旋结构、二级结构和三级结构的变化程度、多肽分子量降解的速度有所差异;盐离子强度(0~150 mM)会影响燕麦蛋白纳米纤维的形成,随着盐离子浓度的增强,纳米纤维的平均长度会减小,而直径基本保持一致,但是纤维变得弯曲;当离子强度增加到50 mM或以上时,纳米纤维发生团聚。
通过PEG基团对燕麦分离蛋白进行分子修饰,改变其水溶性等理化性质,并用FTIR和HNMR对修饰产物进行鉴定,结果表明,通过反应能成功将PEG嫁接到燕麦分离蛋白分子上,显著改善了燕麦分离蛋白的水溶性。PEG通过醚的方式结合到了燕麦分离蛋白质OPI上,改性后,红外光谱中OPI-PEG在1105 cm~(-1)处出现较强吸收,为结合醚键吸收,~843, 963, and 2886 cm~(-1)处也出现吸收,为PEG特征吸收。OPI-MPEG蛋白的特征吸收未变,在1658 cm~(-1),1536 cm~(-1)处仍有较强吸收。OPI-MPEG核磁结果显示在3.329 ,3.651,3.598 PPM处出现较强波峰,其他波形相对于OPI未变;修饰后的蛋白分子β-类结构含量降低,对其纳米纤维的形成有抑制作用。
The protein nanofibrils generally thought to be associated with more than 20 diseases ,including several neurodegenerative diseases, such as Parkinson’s and Alzheimer’s and the food protein fibrils could be used as thickening ingredients in low-calorie products, for example, as replacements for polysaccharide-based ingredients or meat replacement products and high protein content foods,also they can be used to accelerate the gel formation and then low the cost of the gel; This study will play a positive role in promoting development of the diseases treatment and health foods.
The amino acid compositions, secondary structure, and self-assembly of the oat protein isolate and oat globulin were studied in this dissertation, and the nanofibrils formation of them were further investigated in the nanoscale; The effect of modification of the protein on nanofibrils formation was also researched after the the water soluble compound PEG-OPI being synthesized using hydrophilic polyethylene glycol monomethyl ether (PEG) substitutions.
The amino acid compositions, secondary structure, and self-assembly of oat protein isolate (OPI), which was purified from the high-protein Chinese oat, have been investigated by using a combination of amino acid analysis, Fourier transform infrared spectroscopy (FTIR), and tapping mode atomic force microscopy (TP-AFM). OPI, with molecular weights ranging from 14.0 kDa to 66.0 kDa, was rich in essential amino acids and contained 24.7% glutamic acid and 8.1% leucine. The amino acid contents of OPI are 4.5?8.7 times higher than those of oat flour. The secondary structures of OPI have been quantified by the deconvolution of the amide I band of the FTIR spectrum of OPI, which were found to contain approximately 7%β-turn, 19%α-helix, and 74%β-sheet. Tapping mode AFM results further suggest that the oat protein isolate has two major types of shapes, ellipsoidal and disk-like. At protein concentrations below 0.5 mg/mL, most of the OPI molecules are in the isolated form. However, when the concentration of OPI reaches 1.0 mg/mL, some of the OPI molecules self-assembled into large and heterogeneous protein aggregates.
The physicochemical and conformational properties, including amino acid composition, subunits, secondary structures, the size and shapes of the individual oat globulin molecule or protein aggregates were evaluated in this study by FTIR, tapping mode AFM, TEM and Dynamic laser light-scattering. Oat globulin, whose molecular weights range from 10.0 KDa to 70.0 KDa, were rich in essential amino acids, and consist of Glutamic acid 24.20% andArginine 8.96%. The amino acid content of oat globulin is 3.78～9.60 times higher than that of oat flour. The secondary structures have been quantified by the deconvolution of the amide I band of the FTIR spectrum of oat globulin, which were found to contain approximately 8.5%β-turn, 10.2%α-helix, and 81.3%β-sheet, which was a bit different from the result of CD spectrum 12.9 %α-helix, 32.8 %β-strand, 25.7%β-turn , and 28.2% random coil, the main difference was theβ-turn and random coil.Tapping mode AFM results and TEM further suggest that the oat globulin has major type of global shape. At protein concentrations below 0.1 mg/mL, most of oat globulin molecules are in the isolated form. However, when the concentration of the protein reaches 0.5 mg/mL, some of the molecules self-assembled into large and heterogeneous protein aggregates. Dynamic laser light-scattering showed that the average radius of the oat globulin was about 39.8nm by simple fit with a range from 6nm-200nm, however,the number or mass weighted showed that the radius of about 6nm took up over 90% of the total, the big radius ones belonged to the aggregations,the result is consist with the AFM and TEM.
We demonstrate that oat globulin is capable of forming regular elongated fibrils with flat ribbon structure about 4~16nm in height and 0~10μm in length at condition of 24 h ,85°C, protein concentration 1-10 mg/ml,pH 2 as judged from transmission electron microscopy (TEM), atomic force microscopy (AFM), binding of thioflavin T (Th T) and Congo Red dyes, and circular dichroism spectroscopy, it shows that The fibril formation could be greatly influenced by the protein concentration, heating time. Significant protein fibril aggregation occurs when the oat protein concentration increases to 5mg/ml from 2 mg/ml.The morphology of the formed fibrils was closely dependent upon heating time from 0 to 24h. The diameters of the fibrils formed at various times were similar, but the mean contour length progressively increased with heating time. The ThT maximum fluorescence also progressively increased with heating time.The heating process caused remarkable changes in secondary, tertiary, and quaternary conformations of the oat globulin. Gel electrophoresis analysis indicated that heating disrupted the polypeptides of oat globulin, leading to the formation of fragments with lower molecular mass (e.g., <20 kDa after 12h). This appears to be the first direct observation of nanofibrils from oat globulin. The viscosity resulted in a significantly increase in compared to the unheated sample after heating.
The morphology fabrication and conformational characteristics of multistranded amyloid-like fibrils as a function of heating time of oat protein isolates (OPI ) were demonstrated by combining of AFM, TEM analysis and DLS techniques, as well as circular dichroism spectroscopy (CD) and SDS-PAGE, as well as binding of thioflavin T (Th T). Results shows that Polydisperse semiflexible nanofibrils with almost the same width can be induced by heating at pH 2.0 from oat protein isolates, and it is suggested that short protofilaments and isolated molecules can touched and aligned with others to developed into a longer contour length ones; Ionic strengths (0–150 mM) had a significant effect on the fibrils formation, the contour length of the stranded aggregates markedly decreased with ionic strength increasing, while the thickness of the strands was nearly unchanged. At ionic strength of 50 mM or above, the stranded aggregates gradually became clustered.
A new protein-based water soluble compound PEG-OPI, has been synthesized using hydrophilic polyethylene glycol monomethyl ether (PEG) substitutions. The success of synthesis was confirmed by FT-IR and 1H NMR spectroscopy. In comparison with OPI, the FT-IR spectrum of MPEG-OPI presented new absorption peaks at ~1105 cm-1, which was assigned to ether groups, as well as ~843, 950, and 2886 cm-1 peaks, which arose from MPEG segmen, peaks corresponding to -COCH2CH2CO- group of MPEG-OPI molecule appeared at 3.598,3.651 ppm on its 1H NMR spectrum, the sharp single-peak signal at 3.329 ppm was assigned to -OCH3 of MPEG segments,the modification inhibited the formation of the fibrils as theβ-turn structure decreased.
本论文以燕麦分离蛋白和燕麦球蛋白为原料,通过氨基酸分析仪、SDS-PAGE、红外光谱仪、园二色谱、敲击式原子力扫描电镜、透射电镜和动态流变仪、动态光散射等研究燕麦分离蛋白和燕麦球蛋白的氨基酸组成、二级结构和聚集等性质;采用原子力扫描电镜和透射电镜在纳米尺度下对影响其纳米纤维形成的理化因素进行比较,并运用多种手段对其纳米纤维的形貌和特性进行表征;通过进一步对燕麦分离蛋白进行分子修饰,达到提高其功能特性的目的,同时深入研究修饰对燕麦分离蛋白纳米纤维形成产生的影响,主要研究结果如下:
燕麦分离蛋白OPI的多肽分子量在14.0 kDa到66.0 kDa之间,谷氨酸和亮氨酸含量分别高达24.7%,8.1%;燕麦分离蛋白含有大约7%β-转曲, 19%α-螺旋,和74%β-折叠;敲击式原子力扫描电镜结果显示燕麦分离蛋白主要以两种形状存在,椭球形和碟盘形;在浓度低于0.5 mg/mL时,OPI分子以单个分子形式存在,当浓度高于1.0 mg/mL时,许多OPI分子相互聚集会形成颗粒大小分布不均匀的聚集体;燕麦球蛋白的多肽分子量在10.0 KDa to 70.0 Kda之间,谷氨酸和精氨酸含量分别高达24.2%和9.0%,红外光谱结果表面,燕麦球蛋白含有大约8.5%β-转曲, 10.2%α-螺旋, 81.3%β-折叠。原子力扫描显微镜结果表明燕麦球蛋白分子主要以椭球形式存在,在球蛋白分子浓度低于0.1 mg/mL时,球蛋白分子以单个分子形式存在,当浓度高于0.5 mg/mL时,球蛋白分子即自组装形成颗粒大小分布不均的聚集体;动态光散射结果表明球蛋白的平均水合半径大约为39.8nm,颗粒大小主要在6nm-200nm之间,其中,水合半径在6nm左右的颗粒数量占总数的90%以上,具有较大水合半径的是球蛋白自组装形成的聚集体,研究结果与原子力扫描电镜和透射电镜结果一致。
燕麦球蛋白分子能在85°C,蛋白浓度1~10 mg/ml, pH 2条件下,加热24小时的过程中形成直径12nm左右,长度0~10μm的纳米纤维,纳米纤维的平均长度与加热时间成正相关,而纤维直径基本保持一致,具有螺旋周期结构;纳米纤维形成过程中燕麦球蛋白分子二级结构和三级结构显著发生变化,同时伴随着多肽链的降解,在12小时后,体系中多肽的分子量降低到<20 kDa以下,β-折叠含量显著增加。
燕麦分离蛋白能在pH2,85°C,搅拌速度400rad/s条件下随着加热时间的延长形成长度0~7μm的纳米纤维,纳米纤维长度分布不均但直径基本相同,具有螺旋周期结构;体系中蛋白分子的水合半径Rh随着加热时间延期逐渐增加;燕麦球蛋白与燕麦分离蛋白的不同之处在于燕麦球蛋白在搅拌速度为0rad/s的情况下也能形成纳米纤维,燕麦球蛋白在同样条件下,纤维的平均长度更长,颗粒形成纤维的转化率更高,纤维的螺旋结构、二级结构和三级结构的变化程度、多肽分子量降解的速度有所差异;盐离子强度(0~150 mM)会影响燕麦蛋白纳米纤维的形成,随着盐离子浓度的增强,纳米纤维的平均长度会减小,而直径基本保持一致,但是纤维变得弯曲;当离子强度增加到50 mM或以上时,纳米纤维发生团聚。
通过PEG基团对燕麦分离蛋白进行分子修饰,改变其水溶性等理化性质,并用FTIR和HNMR对修饰产物进行鉴定,结果表明,通过反应能成功将PEG嫁接到燕麦分离蛋白分子上,显著改善了燕麦分离蛋白的水溶性。PEG通过醚的方式结合到了燕麦分离蛋白质OPI上,改性后,红外光谱中OPI-PEG在1105 cm~(-1)处出现较强吸收,为结合醚键吸收,~843, 963, and 2886 cm~(-1)处也出现吸收,为PEG特征吸收。OPI-MPEG蛋白的特征吸收未变,在1658 cm~(-1),1536 cm~(-1)处仍有较强吸收。OPI-MPEG核磁结果显示在3.329 ,3.651,3.598 PPM处出现较强波峰,其他波形相对于OPI未变;修饰后的蛋白分子β-类结构含量降低,对其纳米纤维的形成有抑制作用。
The protein nanofibrils generally thought to be associated with more than 20 diseases ,including several neurodegenerative diseases, such as Parkinson’s and Alzheimer’s and the food protein fibrils could be used as thickening ingredients in low-calorie products, for example, as replacements for polysaccharide-based ingredients or meat replacement products and high protein content foods,also they can be used to accelerate the gel formation and then low the cost of the gel; This study will play a positive role in promoting development of the diseases treatment and health foods.
The amino acid compositions, secondary structure, and self-assembly of the oat protein isolate and oat globulin were studied in this dissertation, and the nanofibrils formation of them were further investigated in the nanoscale; The effect of modification of the protein on nanofibrils formation was also researched after the the water soluble compound PEG-OPI being synthesized using hydrophilic polyethylene glycol monomethyl ether (PEG) substitutions.
The amino acid compositions, secondary structure, and self-assembly of oat protein isolate (OPI), which was purified from the high-protein Chinese oat, have been investigated by using a combination of amino acid analysis, Fourier transform infrared spectroscopy (FTIR), and tapping mode atomic force microscopy (TP-AFM). OPI, with molecular weights ranging from 14.0 kDa to 66.0 kDa, was rich in essential amino acids and contained 24.7% glutamic acid and 8.1% leucine. The amino acid contents of OPI are 4.5?8.7 times higher than those of oat flour. The secondary structures of OPI have been quantified by the deconvolution of the amide I band of the FTIR spectrum of OPI, which were found to contain approximately 7%β-turn, 19%α-helix, and 74%β-sheet. Tapping mode AFM results further suggest that the oat protein isolate has two major types of shapes, ellipsoidal and disk-like. At protein concentrations below 0.5 mg/mL, most of the OPI molecules are in the isolated form. However, when the concentration of OPI reaches 1.0 mg/mL, some of the OPI molecules self-assembled into large and heterogeneous protein aggregates.
The physicochemical and conformational properties, including amino acid composition, subunits, secondary structures, the size and shapes of the individual oat globulin molecule or protein aggregates were evaluated in this study by FTIR, tapping mode AFM, TEM and Dynamic laser light-scattering. Oat globulin, whose molecular weights range from 10.0 KDa to 70.0 KDa, were rich in essential amino acids, and consist of Glutamic acid 24.20% andArginine 8.96%. The amino acid content of oat globulin is 3.78～9.60 times higher than that of oat flour. The secondary structures have been quantified by the deconvolution of the amide I band of the FTIR spectrum of oat globulin, which were found to contain approximately 8.5%β-turn, 10.2%α-helix, and 81.3%β-sheet, which was a bit different from the result of CD spectrum 12.9 %α-helix, 32.8 %β-strand, 25.7%β-turn , and 28.2% random coil, the main difference was theβ-turn and random coil.Tapping mode AFM results and TEM further suggest that the oat globulin has major type of global shape. At protein concentrations below 0.1 mg/mL, most of oat globulin molecules are in the isolated form. However, when the concentration of the protein reaches 0.5 mg/mL, some of the molecules self-assembled into large and heterogeneous protein aggregates. Dynamic laser light-scattering showed that the average radius of the oat globulin was about 39.8nm by simple fit with a range from 6nm-200nm, however,the number or mass weighted showed that the radius of about 6nm took up over 90% of the total, the big radius ones belonged to the aggregations,the result is consist with the AFM and TEM.
We demonstrate that oat globulin is capable of forming regular elongated fibrils with flat ribbon structure about 4~16nm in height and 0~10μm in length at condition of 24 h ,85°C, protein concentration 1-10 mg/ml,pH 2 as judged from transmission electron microscopy (TEM), atomic force microscopy (AFM), binding of thioflavin T (Th T) and Congo Red dyes, and circular dichroism spectroscopy, it shows that The fibril formation could be greatly influenced by the protein concentration, heating time. Significant protein fibril aggregation occurs when the oat protein concentration increases to 5mg/ml from 2 mg/ml.The morphology of the formed fibrils was closely dependent upon heating time from 0 to 24h. The diameters of the fibrils formed at various times were similar, but the mean contour length progressively increased with heating time. The ThT maximum fluorescence also progressively increased with heating time.The heating process caused remarkable changes in secondary, tertiary, and quaternary conformations of the oat globulin. Gel electrophoresis analysis indicated that heating disrupted the polypeptides of oat globulin, leading to the formation of fragments with lower molecular mass (e.g., <20 kDa after 12h). This appears to be the first direct observation of nanofibrils from oat globulin. The viscosity resulted in a significantly increase in compared to the unheated sample after heating.
The morphology fabrication and conformational characteristics of multistranded amyloid-like fibrils as a function of heating time of oat protein isolates (OPI ) were demonstrated by combining of AFM, TEM analysis and DLS techniques, as well as circular dichroism spectroscopy (CD) and SDS-PAGE, as well as binding of thioflavin T (Th T). Results shows that Polydisperse semiflexible nanofibrils with almost the same width can be induced by heating at pH 2.0 from oat protein isolates, and it is suggested that short protofilaments and isolated molecules can touched and aligned with others to developed into a longer contour length ones; Ionic strengths (0–150 mM) had a significant effect on the fibrils formation, the contour length of the stranded aggregates markedly decreased with ionic strength increasing, while the thickness of the strands was nearly unchanged. At ionic strength of 50 mM or above, the stranded aggregates gradually became clustered.
A new protein-based water soluble compound PEG-OPI, has been synthesized using hydrophilic polyethylene glycol monomethyl ether (PEG) substitutions. The success of synthesis was confirmed by FT-IR and 1H NMR spectroscopy. In comparison with OPI, the FT-IR spectrum of MPEG-OPI presented new absorption peaks at ~1105 cm-1, which was assigned to ether groups, as well as ~843, 950, and 2886 cm-1 peaks, which arose from MPEG segmen, peaks corresponding to -COCH2CH2CO- group of MPEG-OPI molecule appeared at 3.598,3.651 ppm on its 1H NMR spectrum, the sharp single-peak signal at 3.329 ppm was assigned to -OCH3 of MPEG segments,the modification inhibited the formation of the fibrils as theβ-turn structure decreased.
引文
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