基于QCM技术的血浆蛋白和血小板吸附行为研究
摘要
本论文主要采用QCM技术研究了几种主要血浆蛋白:白蛋白(HSA),免疫球蛋白(IgG)和纤维蛋白原(FGN),在材料表面的吸附行为和刚性(单层)吸附条件,白蛋白和纤维蛋白原以及血小板在Ti和Au表面的吸附行为比较,探讨了血浆蛋白予吸附对血小板吸附的影响;采用接触角测量,光学显微镜和原子力显微镜(AFM)对吸附底表面、吸附蛋白和吸附血小板进行了检测,通过本研究以期进一步揭示界面生物大分子的吸附行为,指导抗凝血材料的设计。
1.以Au为吸附底模型材料,利用QCM技术研究了HSA,IgG和FGN的吸附行为:分别研究了温度、浓度和pH对单一血浆蛋白吸附的影响。结果表明在温度为25℃,pH为7.0的条件下,三种蛋白刚性吸附浓度分别为:20μg/ml、10μg/ml和10μg/ml,为单层吸附;温度为25℃和37℃的条件对HSA和FGN的吸附影响差异不明显,而对IgG的影响较为明显;对不同pH结果显示,在等电点处具有最大的吸附量和层厚;水分子的嵌合会增加蛋白吸附单层的柔性。
2.以Au为吸附底模型材料,利用QCM技术研究了在温度为25℃,pH为7.0,刚性吸附浓度条件下蛋白的竞争吸附行为。结果表明不同蛋白的竞争吸附依赖于所选蛋白体系,在二元蛋白体系中,HSA和IgG之间无明显竞争吸附,FGN的吸附强与HSA;在顺次通入时,FGN的吸附强于IgG,而在按比例通入时,IgG的吸附强于FGN。在三元混合蛋白体系中,HSA和IgG的吸附强于FGN。不同蛋白的结构和相互之间的作用以及水合作用会导致刚性或柔性吸附行为。
3.利用QCM技术研究了HSA和FGN在Au和Ti表面的不同吸附行为。结果表明FGN在Au表面较在Ti表面吸附量大,均呈刚性吸附。HSA在Ti表面较在Au表面吸附量大,在Au表面呈刚性吸附,而在Ti表面呈柔性吸附,包含较多水分子。不同蛋白的吸附与材料表面的浸润性存在一定关系。
4.利用QCM技术研究了血小板在予吸附FGN和未予吸附FGN的Au和Ti表面的吸附行为。结果表明血小板在未予吸附FGN的Ti表面的吸附量要少于在Au表面的,在Ti表面呈刚性吸附,无构象变化发生,在Au表面呈柔性吸附,有一定构象变化。予吸附FGN对血小板在Au表面的吸附存在一定的抑制作用,但是却增加了在Ti表面的吸附量。血小板在予吸附FGN后的Ti表面的吸附量比Au表面的大。在予吸附FGN的Au表面呈刚性吸附,而在Ti表面呈柔性吸附。FGN在Ti表面的予吸附对血小板的吸附影响较大。需要进一步研究证实。
In this thesis,QCM technique is used to study the adsorption behavior and rigidity condition of plasma protein,e.g.Human Serum Albumin(HSA), Immunoglobin G(IgG)and Fibrinogen(FGN),on material's surface,the adsorption comparison of HSA,FGN and platelet on Ti and Au crystals,and the influence of pre-adsorbed FGN on platelet adhesion.Contact angle test,Atomic Force Microscopy(AFM)and Optical Microscopy are used to investigate the wettability of adsorption substrate and the morphology of adsorbed protein and platelet.In order to reveal the adsorption behavior of biomolecules at interface and guide the design of anticoagulation biomaterials.
1.The adsorption behavior of HSA,IgG and FGN on Au crystal is studied using QCM.The influence of Temperature,Concentration and pH on single plasma protein is also investigated.The results show that the concentration for rigidity adsorption at 25℃,pH～7.0 is 20μg/ml,10μg/ml and 10μg/ml for the three proteins,respectively,and a monolayer formation.There is no significant difference for the adsorption of HSA and FGN at different temperature such as 25℃and 37℃,while significant for IgG..Each protein has the largest adsorption mass and thickness at pI and the trapped water can increase the flexibility of the protein monolayer.
2.The competitive adsorption behavior among the three proteins is studied on Au crystal by QCM under the condition:25℃,pH～7.0 and rigidity adsorption concentration.The results show that the competitive adsorption depends on different protein system.In binary system,there is no obvious competition between HSA and IgG,the adsorption of FGN is stronger than HSA.While in due course adsorption,FGN is stronger than IgG,and in mixed course adsorption, IgG is stronger than FGN.In tenary system,HSA and IgG are stronger than FGN. The rigidity or soft adsorption behavior is observed due to the different structure, the interaction and hydration of protein.
3.The different adsorption behavior of HSA and FGN is studied by QCM.The results show that FGN has larger adsorption on Au than on Ti,and both show rigidity adsorption.HSA has larger adsorption on Ti than on Au,and shows soft layer with trapped water,while rigidity on Au.There is relationship between wettability of materials and protein adsorption.
4.The platelet adsorption behavior on un-preadsorption FGN and preadsorption FGN Au and Ti surfaces is studied.The results show that there are less platelets on un-preadsorption FGN Ti than on Au,and platelets on Ti are rigidity without conformational change,while soft on Au with comformational change.There is inhibition of platelet adsorption on preadsorption FGN Au surface,and the adsorbates are rigid,while more platelets adsorbed on preadsorption FGN Ti surface with flexibility.There is a large influence of preadsorption FGN on platelet adhesion on Ti surface,which need further investigation.
1.以Au为吸附底模型材料,利用QCM技术研究了HSA,IgG和FGN的吸附行为:分别研究了温度、浓度和pH对单一血浆蛋白吸附的影响。结果表明在温度为25℃,pH为7.0的条件下,三种蛋白刚性吸附浓度分别为:20μg/ml、10μg/ml和10μg/ml,为单层吸附;温度为25℃和37℃的条件对HSA和FGN的吸附影响差异不明显,而对IgG的影响较为明显;对不同pH结果显示,在等电点处具有最大的吸附量和层厚;水分子的嵌合会增加蛋白吸附单层的柔性。
2.以Au为吸附底模型材料,利用QCM技术研究了在温度为25℃,pH为7.0,刚性吸附浓度条件下蛋白的竞争吸附行为。结果表明不同蛋白的竞争吸附依赖于所选蛋白体系,在二元蛋白体系中,HSA和IgG之间无明显竞争吸附,FGN的吸附强与HSA;在顺次通入时,FGN的吸附强于IgG,而在按比例通入时,IgG的吸附强于FGN。在三元混合蛋白体系中,HSA和IgG的吸附强于FGN。不同蛋白的结构和相互之间的作用以及水合作用会导致刚性或柔性吸附行为。
3.利用QCM技术研究了HSA和FGN在Au和Ti表面的不同吸附行为。结果表明FGN在Au表面较在Ti表面吸附量大,均呈刚性吸附。HSA在Ti表面较在Au表面吸附量大,在Au表面呈刚性吸附,而在Ti表面呈柔性吸附,包含较多水分子。不同蛋白的吸附与材料表面的浸润性存在一定关系。
4.利用QCM技术研究了血小板在予吸附FGN和未予吸附FGN的Au和Ti表面的吸附行为。结果表明血小板在未予吸附FGN的Ti表面的吸附量要少于在Au表面的,在Ti表面呈刚性吸附,无构象变化发生,在Au表面呈柔性吸附,有一定构象变化。予吸附FGN对血小板在Au表面的吸附存在一定的抑制作用,但是却增加了在Ti表面的吸附量。血小板在予吸附FGN后的Ti表面的吸附量比Au表面的大。在予吸附FGN的Au表面呈刚性吸附,而在Ti表面呈柔性吸附。FGN在Ti表面的予吸附对血小板的吸附影响较大。需要进一步研究证实。
In this thesis,QCM technique is used to study the adsorption behavior and rigidity condition of plasma protein,e.g.Human Serum Albumin(HSA), Immunoglobin G(IgG)and Fibrinogen(FGN),on material's surface,the adsorption comparison of HSA,FGN and platelet on Ti and Au crystals,and the influence of pre-adsorbed FGN on platelet adhesion.Contact angle test,Atomic Force Microscopy(AFM)and Optical Microscopy are used to investigate the wettability of adsorption substrate and the morphology of adsorbed protein and platelet.In order to reveal the adsorption behavior of biomolecules at interface and guide the design of anticoagulation biomaterials.
1.The adsorption behavior of HSA,IgG and FGN on Au crystal is studied using QCM.The influence of Temperature,Concentration and pH on single plasma protein is also investigated.The results show that the concentration for rigidity adsorption at 25℃,pH～7.0 is 20μg/ml,10μg/ml and 10μg/ml for the three proteins,respectively,and a monolayer formation.There is no significant difference for the adsorption of HSA and FGN at different temperature such as 25℃and 37℃,while significant for IgG..Each protein has the largest adsorption mass and thickness at pI and the trapped water can increase the flexibility of the protein monolayer.
2.The competitive adsorption behavior among the three proteins is studied on Au crystal by QCM under the condition:25℃,pH～7.0 and rigidity adsorption concentration.The results show that the competitive adsorption depends on different protein system.In binary system,there is no obvious competition between HSA and IgG,the adsorption of FGN is stronger than HSA.While in due course adsorption,FGN is stronger than IgG,and in mixed course adsorption, IgG is stronger than FGN.In tenary system,HSA and IgG are stronger than FGN. The rigidity or soft adsorption behavior is observed due to the different structure, the interaction and hydration of protein.
3.The different adsorption behavior of HSA and FGN is studied by QCM.The results show that FGN has larger adsorption on Au than on Ti,and both show rigidity adsorption.HSA has larger adsorption on Ti than on Au,and shows soft layer with trapped water,while rigidity on Au.There is relationship between wettability of materials and protein adsorption.
4.The platelet adsorption behavior on un-preadsorption FGN and preadsorption FGN Au and Ti surfaces is studied.The results show that there are less platelets on un-preadsorption FGN Ti than on Au,and platelets on Ti are rigidity without conformational change,while soft on Au with comformational change.There is inhibition of platelet adsorption on preadsorption FGN Au surface,and the adsorbates are rigid,while more platelets adsorbed on preadsorption FGN Ti surface with flexibility.There is a large influence of preadsorption FGN on platelet adhesion on Ti surface,which need further investigation.
引文
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[2].周长忍.生物材料学.中国医药科技出版社.2004.1-2.
[3].顾汉卿,徐国风.生物医学材料学[M].天津:天津科技翻译出版社.1993.40-45.
[4].N.Huang,13th International Conference on Surface Modification Technologies,8-10 Sept.1999,SINGAPORE:207-220.
[5].N.Huang,5th Asia Symposium on biomedical materials,2001,12,9-12,Hong Kong.
[6].俞耀庭,张兴栋,生物医用材料.天津:天津大学出版社,2000.
[7].黄嘉,乐以伦,生物医学工程杂志,1999,16(3):371.
[8].胡国栋.国外医学生物医学工程分册,2002,25(6):271-273.
[9].J.GSteele,G.Johnson,W.D.Norris,Biomaterials,1991,12:531.
[10].俞凯,陈治清.生物医学工程杂志,1996,13(3):189.
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[16].Y.Tamada.E.A.Kulik.Biomaterials,1995.16:259-261.
[17].王多宁,赵雁武.考马斯亮蓝微盘比色法测定蛋白质含量[J].第四军医大学学报,2001,22(6):528-529.
[18].Guenther H O.Measuration of protein in milk using immune method [J].Lebensmittel Chem.,1991,4(1):145-167.
[19].Xia Chu,Zi Long Zhao,Guo Li Shen.Quartz crystal microbalance immunoassay with dendritic amplification,using colloidal gold immunocomplex[J].Sensors and Actuators B,2006,114(6):696-704.
[20].Karin Glasmastar,Charlotte Larsson,Fredrik Hook.Protein Adsorption on Supported Phospholipid Bilayers[J].Journal of Colloid and Interface Science,2002,246(5):40-47.
[21].Ning Luo,Chun Zhang,Douglas E.Hirt.Adsorption of fluorescently labeled protein residues on poly(ethylene-co-acrylic acid)films modified with affinity functionalities.Colloids and Surfaces B:Biointerfaces,2006,50(9):89-96.
[22].张爱宏,刘国庆.放射性同位素标记法检测脂蛋白脂肪酶活性及其应用[J].中国动脉硬化杂志,2003,11(6):573-576.
[23]H.Fitzpatrick,P.F.Luckham,S.Eriksen,K.J.Hammond,J.Col Inter Sci.149(1992)1.
[24].F.Hook,J.Voros,M.Rodahl.A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry,optical waveguide lightmode spectroscopy,and quartz crystal microbalance/dissipation.[J]Colloids and Surfaces B:Biointerfaces,2002,24(3):155-170.
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