BSA与羟磷灰石相互吸附的FTIR-ATR光谱

doi:10.3866/PKU.WHXB201511301

摘要/Abstract

摘要：

采用傅里叶变换红外衰减全反射(FTIR-ATR)光谱法对牛血清白蛋白(BSA)在羟磷灰石(HA)[Ca₁₀(OH)₂(PO₄)₆]表面不同时间的相互吸附作用进行了表征。在BSA溶液作用下,羟磷灰石表面的Ca²⁺、PO₄^3-和OH^-离子初始的溶解和再沉淀使得BSA与HA相互作用层层叠加,在HA表面形成从表层到次表层分子都包含有吸附的BSA的覆盖层,从而加深两者之间的相互作用。经红外差谱法处理过的相关ATR数据表明, BSA与HA之间的相互作用是快速的,并随时间变化进一步加强;来自HA上PO₄^3-的P=O基团对蛋白质肽键的酰胺II带(―CNH)、多肽链的甲基(―PO₃)和亚甲基(―CH₂)上氢的吸附作用要比P―O快速而且强烈。Ca²⁺在该吸附过程中起了极其重要的作用,其快速与蛋白质肽键的羰基氧发生作用,并诱导该蛋白质二级结构由β-折叠向α-螺旋和β-转角构象转变;伴随着这一构象变化,蛋白质多肽链上大多数肽键的―C=O和H―N―活性基团从链间氢键交联中释放出来,带动众多的氢分别参与同HA表面的Ca²⁺、PO43-和OH^-离子的相互吸附作用,并牢牢地结合于HA表面;这对硬组织的再生起着重要作用,促进了HA的生物矿化过程。

关键词: 生物材料, 蛋白质吸附作用, 多肽, 红外光谱, FTIR-ATR, 生物矿化作用

Abstract:

The microcosmic process of bovine serum albumin (BSA) adsorbing onto hydroxyapatite (HA) for different time intervals was investigated by Fourier transform infrared attenuated total internal reflectance (FTIRATR) spectrometry. The initial dissolution and re-precipitation of PO₄^3-, Ca²⁺, and OH^- ions from the HA coating led to the occurrence of the coating including adsorbed BSA on the HA from surface-to subsurface-molecular layers and to in-depth interaction between BSA and HA. The subtraction results gained in the adsorption regions of HA and BSA reveal that the binding of P=O, from the phosphate (PO₄^3-), to the hydrogen of amide II, methyl and methene of the BSA appears to be considerably more rapid and stronger than that of the P―O group. In addition, it is very likely that Ca²⁺ plays an important role in the interaction of BSA with HA. It appears that the binding of Ca²⁺ to the carbonyl-oxygen of the peptide bond in BSAcaused a significant, molecular, conformational rearrangement of polypeptide backbones from β-pleated sheet to helical circles of α-helix and β-turn. This change appears to have been followed by much hydrogen of polypeptides being driven to bind PO₄^3- and OHeffectively and much ―C=O and H―N―groups of the peptide bond being freed from inter-chain hydrogenbonding to act on Ca²⁺ and combine strongly with the HA surface. This might reasonably be expected to promote hard tissue regeneration. BSA seems to be activated by the inductive effect of Ca²⁺ via the molecular rearrangement of polypeptide backbones from pleated sheet to helical circles and in turn reacts strongly on the HA, resulting in profound effects on the course of biomineralization.

Key words: Biomaterial, Protein adsorption, Polypeptide, IR spectroscopy, FTIR-ATR, Biomineralization

叶青,胡仁,周剑章,叶艺文,许朝曦,林昌健,林种玉. BSA与羟磷灰石相互吸附的FTIR-ATR光谱[J]. 物理化学学报, 2016, 32(2), 565-572. doi: 10.3866/PKU.WHXB201511301

Qing YE,Ren HU,Jian-Zhang ZHOU,Yi-Wen YE,Zhao-Xi XU,Chang-Jian LIN,Zhong-Yu LIN. FTIR-ATR Spectrometry of BSA Adsorption on Hydroxyapatite[J]. Acta Phys. -Chim. Sin. 2016, 32(2), 565-572. doi: 10.3866/PKU.WHXB201511301

链接本文: https://www.whxb.pku.edu.cn/CN/10.3866/PKU.WHXB201511301

https://www.whxb.pku.edu.cn/CN/Y2016/V32/I2/565

参考文献

1	Moulton S. E. ; Barisci J. N. ; McQuillan A. J. ; Wallace G. G Colloid. Surf. A: Physicochem. Eng. Asp 2003, 220, 159.
2	Lenk T. J. ; Ratner B. D. ; Gendreau R. M. ; Chittur K. K J. Biomed. Mater. Res 1989, 23, 549.
3	Shen Y. H. ; Yang Z. L. ; Wu J. G Acta Phys. -Chim. Sin 1999, 15 (12), 1064.
3	沈玉华; 杨展澜; 吴瑾光. 物理化学学报, 1999, 15 (12), 1064.
4	Shen, Y. H.; Yang, Z. L.; Wu, J. G. 1999, 35 (4), 431.
4	沈玉华,杨展澜,吴瑾光.北京大学学报(自然科学版), 1999, 35 (4), 431.
5	Elangovan S. ; Margolis H. C. ; Oppenheim F. G. ; Beniash E Langmuir 2007, 23 (22), 11200.
6	Ong J. L. ; Chittur K. K. ; Lucas L. C. J Biomed. Mater. Res 1994, 28, 1337.
7	Yang Q. ; Zhang Y. Y. ; Liu M. L. ; Ye M. ; Zhang Y. Q. ; Yao S. Z Analytica Chimica Acta 2007, 597, 58.
8	Zeng H. T. ; Chittur K. K. ; Lacefield W. R Biomaterials 1999, 20, 377.
9	Feng B. ; Chen J. Y. ; Zhang X. D Biomaterials 2002, 23 (12), 2499.
10	Ye Q. ; Hu R. ; Lin Z. Y. ; Lin C. J. Chem. J. Chin. Univ 2006, 27 (8), 1552.
10	叶青; 胡仁; 林种玉; 林昌健. 高等学校化学学报, 2006, 27 (8), 1552.
11	Yan, Y. L.; Jin, Z. C. Applications of Fourier TransformInfrared Spectrometry in Researches of Agriculture, Food andBiology. In Modern Fourier-Transform Infrared Spectrometry and Its Applications (Part II); 1st ed.; Wu, J. G. Ed.; Literatureof Science and Technology Press: Beijing, 1994; pp 177-180.
11	严衍禄,金泽宸.傅里叶变换光谱在农业、食品和生物学研究中的应用;近代傅里叶变换红外光谱技术及应用(下卷).吴瑾光主编.北京:科学技术文献出版社, 1994: 177-180.
12	Maruyama T. ; Katoh S. ; Nakajima M. ; Nabetani H. ; Abbott T. P. ; Shono A. ; Satoh K. J Membr. Sci 2001, 192, 201.
13	Bellamy, L. J. The Infra-red Spectra of Complex Molecules, 3rd ed.; Chapman and Hall: London, 1975; pp 14-26, 107-125, 183-202, 386.
14	Silverstein, R. M.; Bassler, G. C.; Morrill, T. C. Infraredspectrometry. In Spectrometric Identification of Organic Compounds, 5th ed.; Sawicki, D., Stiefel, J. Eds.; Wiley: NewYork, 1991; pp 103, 123.
15	Rao, C. N. R. Chemical applications of Infrared Spectroscopy.1st ed.; Academic Press Inc.: New York, 1963; pp 131-138, 255-262, 480-495.
16	Driessens F. C. M. ; van Dijk J.W. E. ; Borggreven J. M. P. M Calcif. Tissue Res 1978, 26, 127.
17	Clark G. C. F. ; Williams D. F. J Biomed. Mater. Res 1982, 16 (2), 125.
18	Ong J. L. ; Lucas L. C Biomaterials 1998, 19 (4-5), 455.
19	Margolis H. C. ; Moreno E. C Calcif. Tissue Int 1992, 50 (2), 137.
20	Chittur, K. K. Biomaterials 1998, 19 (4-5), 357. doi: 10.1016/S0142-9612(97)00223-8
21	Zhou, J. M.; Shi, N. Applications of Fourier TransformInfrared Spectrometry in Biochemistry. In Modern Fouriertransform Infrared Spectrometry and Its Applications (Part II), 1st ed.; Wu, J. G. Ed.; Literature of Science and TechnologyPress: Beijing, 1994; pp 193-212.
21	周筠梅,施鼐.傅里叶变换红外光谱在生物化学中的应用;近代傅里叶变换红外光谱技术及应用(下卷).吴瑾光主编.北京:科学技术文献出版社, 1994: 193-212.
22	Alvarez J. ; Haris P. I. ; Lee D. C. ; Chapman D. Biochimica Et Biophysica Acta 1987, 916 (1), 5.
23	Xu, C. F. Proteins. In Biochemistry (Book One), 2nd ed.; Shen, T.; Wang, J. Y. Eds.; Higher Education Press: Beijing, 1990; pp 146-150.
23	徐长法.生物化学(上册).沈同,王镜岩主编.北京:高等教育出版社, 1990: 146-150.
24	Hauschka P. V Haemostasis 1986, 16 (3-4), 258.
25	Prestrelski S. J. ; Byler D. M. ; Thompson M. P Biochemistry 1991, 30 (36), 8797.
26	Fronticelli C. ; Bucci E. ; Shamoo A. E Biophys. Chem 1984, 19 (3), 255.
27	Inesi G Annu. Rev. Physiol 1985, 47, 573.
28	Wu G. R. ; Gao Z. Y. ; Dong A. C. ; Yu S. N. Int. J. Biol. Macromol 2012, 50 (4), 1011.
29	Zhao Y.W. ; Yang H. Y. ; Meng K. J. ; Yu S. N. Int. J. Biol. Macromol 2014, 64, 453.
30	Yu, M. M. Hormones. In Biochemistry (Book One), 2nd ed.; Shen, T., Wang, J. Y. Eds.; Higher Education Press: Beijing, 1990; pp 447-455.
30	俞梅敏.生物化学(上册).沈同,王镜岩主编.北京:高等教育出版社, 1990: 447-455.
31	Morrissey B.W. ; Stromberg R. R. J Colloid. Interface Sci 1974, 46 (1), 152.
32	Lin Z. Y. ; Xue R. ; Ye Y.W. ; Zheng J. H. ; Xu Z. L BMC Biotechnol 2009, 9, 62.
33	Lin Z. Y. ; Ye Y.W. ; Li Q. L. ; Xu Z. L. ; Wang M BMC Biotechnol 2011, 11, 98.
34	Zhou, W. J.; Wang, Y. Applications of Infrared Spectrometry inBasic Researches of Inorganic and Coordination Chemistry. InModern Fourier-transform Infrared Spectrometry and Its Applications (Part II), 1st ed.; Wu, J. G. Ed.; Literature ofScience and Technology Press: Beijing, 1994; pp 292-296.
34	周维金,王毅.红外光谱法在无机和配位化学基础研究中的应用;近代傅里叶变换红外光谱技术及应用(下卷).吴瑾光主编.北京:科学技术文献版社, 1994: 292-296.
35	Barth A Prog. Biophys. Mol. Biol 2000, 74 (3-5), 141.
36	Farkas V. ; Vass E. ; Hanssens I. ; Majer Z. ; Hollosi M Bioorg. Med. Chem 2005, 13 (17), 5310.
37	Rahmelow K. ; Hübner W. ; Ackermann T. Anal. Biochem 1998, 257 (1), 1.
38	Shai Y Biochim. Biophys. Acta-Biomembr 2013, 1828 (10), 2306.
39	Kay M. I. ; Young R. A. ; Posner A. S Nature 1964, 204, 1050.
40	Hauschka P. V. ; Carr S. A Biochemistry 1982, 21 (10), 2538.
41	Hauschka, P. V. Osteocalcin and Its Functional Domains. InThe Chemistry and Biology of Mineralized Tissues; Butler, W.T. Ed.; EBSCO Media: Birmingham, 1985; pp 149-158.
42	Horbett, T. A. Protein Adsorption on Biomaterials. InBiomaterials: Interface Phenomena and Applications; Cooper, S. L., Peppas, N. A. Eds.; American Chemical Society:Washington DC, 1982; pp 233-244.
43	Davies, J. E. The importance and Measurement of SurfaceCharge Species in Cell Behavior at the Biomaterial Interface.In Surface Characterization of Biomaterials; Ratner, B. D.Ed.; Elsevier: Amsterdam, 1988; pp 219-222.
44	Ono I. ; Gunji H. ; Kaneko F. ; Saito T. ; Kuboki Y J. Craniofac. Surg 1995, 6 (3), 238.
45	El-Ghannam, A.; Ducheyne, P.; Shapiro, I. M. Trans 21st Annual Meeting of Society for Biomaterials 1995, 46.
46	Gungormus M. ; Fong H. ; Kim I.W. ; Evans J. S. ; Tamerler C. ; Sarikaya M Biomacromolecules 2008, 9 (3), 966.

[1]	刘苗苗, 王文娟, 郝秀萍, 董晓燕. Aβ40和hIAPP在溶液和表面的成核与交叉成核聚集行为[J]. 物理化学学报, 2022, 38(3): 2002024 - .
[2]	陈灵珊, 洪苑秀, 贺石生, 范震, 杜建忠. 聚(ε-己内酯)-多肽共聚物胶束增强抗生素的抗菌活性[J]. 物理化学学报, 2021, 37(10): 1910059 - .
[3]	王苗, 郑虹宁, 许菲. 异氰酸苯酯诱导的类胶原多肽自组装[J]. 物理化学学报, 2021, 37(10): 1911039 - .
[4]	涂昆芳, 李广, 姜艳霞. 温度对乙醇电催化氧化的影响[J]. 物理化学学报, 2020, 36(8): 1906026 - .
[5]	曹傲能. 蛋白质结构的“限域下最低能量结构片段”假说与蛋白质进化的“石器时代”[J]. 物理化学学报, 2020, 36(1): 1907002 - .
[6]	尹玥琪,蒋梦绪,刘春光. Keggin型多酸负载的单原子催化剂(M₁/POM, M = Ni, Pd, Pt, Cu, Ag, Au, POM = [PW₁₂O₄₀]^3-)活化氮气分子的密度泛函理论计算研究[J]. 物理化学学报, 2018, 34(3): 270 -277 .
[7]	莫周胜,秦玉才,张晓彤,段林海,宋丽娟. 环己烯对噻吩在CuY分子筛上吸附的影响机制[J]. 物理化学学报, 2017, 33(6): 1236 -1241 .
[8]	袁康,周雪,杜建忠. 基于多肽和温敏聚合物的光交联囊泡的制备及表征[J]. 物理化学学报, 2017, 33(4): 656 -660 .
[9]	于海洋,王昉,刘其春,马青玉,顾正桂. 新型丝素蛋白膜的结构和热分解动力学机理[J]. 物理化学学报, 2017, 33(2): 344 -355 .
[10]	陈海龙,边红涛,郑俊荣. 基于超快多维振动光谱技术解析分子体系的三维空间构型[J]. 物理化学学报, 2017, 33(1): 40 -62 .
[11]	万昭敏,魏星,彭伟,尹征磊,肖丽,庄林. Pb²⁺促进乙醇氧化C―C键断裂的在线电化学透射红外光谱研究[J]. 物理化学学报, 2016, 32(6): 1467 -1472 .
[12]	周瑜,徐静,王楠楠,尉志武. 超额光谱及其研究进展[J]. 物理化学学报, 2016, 32(1): 239 -248 .
[13]	杨帆, 于鹏云, 赵娟, 赵岩, 王建平. 乙二醇的分子间氢键结构动力学的飞秒非线性红外光谱[J]. 物理化学学报, 2015, 31(7): 1275 -1282 .
[14]	梁菊, 来丹玉, 吴文澜, 李国芝, 李军波, 方财林. 三条两亲性多肽的自组装行为及酸敏特性[J]. 物理化学学报, 2015, 31(4): 722 -728 .
[15]	张畅, 秦玉才, 高雄厚, 张海涛, 莫周胜, 初春雨, 张晓彤, 宋丽娟. Ce改性对Y型分子筛酸性及其催化转化性能的调变机制[J]. 物理化学学报, 2015, 31(2): 344 -352 .