Abstract
The specific interaction between angiogenin and aptamer has been investigated by using AFM. The specificity of the interaction is revealed by comparing the binding probability of aptamer to other elements in a series of control experiments. The results have shown that there is specific interaction force between angiogenin and aptamer. Moreover, the single molecular pull-off force between angiogenin and aptamer has also been determined using the Poisson statistical method to be 133.7±11.7 pN. These findings obtained are helpful to the better revelation of recognition mechanism between angiogenin and aptamer, which provided basis for further understanding the inhibition of the aptamer to angiogenic activity.
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Fett J W, Strydom D J, Lobb R R, et al. Isolation and characterization of angiogenin, an angiogenic protein from human carcinoma cells. Biochem, 1985, 24(20): 5480–5486
Shapiro R, Strydom D J, Olson K A, et al. Isolation of angiogenin from normal human plasma. Biochem, 1987, 26(16): 5141–5146
Bai D Y, Ma H D. The role of angiopoietin in angiogenesis. Acta Academiae Medicinae CPAPF (in Chinese), 2005, 14(4): 323–325
Ahmad S A, Liu W, Jung Y D, et al. The effects of angiopoietin-1 and -2 on tumor growth and angiogenesis in human colon cancer. Cancer Res, 2001, 61(4): 1255–1259
Eggert A, Ikegaki N, Kwiatkowski J, et al. High-level expression of angiogenic factors is associated with advanced tumor stage in human neuroblastomas. Clin Cancer Res, 2000, 6(5): 1900–1908
Papapetropoulos A, Fulton D, Mahboubi K, et al. Angiopoietin-1 inhibits endothelial cell apoptosis via the Akt/ survivin pathway. J Biol Chem, 2000, 275(13): 9102–9105
Wurmbach J H, Hammerer P, Sevine S, et al. The expression of angiopoietins and their receptor Tie-2 in human prostate carcinoma. Anticancer Res, 2000, 20: 5217–5220
Gao D L, Guo K M, Seng J J, et al. Expression of angtopoietin-2 and Tie-2 in gastric carcinoma tissues. Journal of Medical Forum (in Chinese), 2005, 26(20): 40–41
Nobile V, Russo N, Hu G F, et al. Inhibition of human angiogenin by DNA aptamers: nuclear colocalization of an angiogenin-inhibitor complex. Biochem. 1998, 37(19): 6857–6863
Li Y X, He F C. The methods for studies of interaction between DNA and proteins. Chemistry of Life (in Chinese), 2003, 23(4): 306–308
Yang L, Wang K M, Tan W H, et al. Atomic force microscopy study of different effects of natural and semi-synthetic beta-lactam on the cell envelope of Escherichia coli. Anal Chem. 2006, 78: 7341–7345
Yamashina S, Shigeno M. Application of atomic force microscopy to ultrastructural and histochemical studied of fixed and embedded cells. J Electron Microsc, 1995, 44(6): 462–466
Mingorance J, Tadros M, Vicente M, et al. Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy. J Biol Chem, 2005, 280(21): 20909–20914
Wang Z G, Wan L J, Zhou C Q, et al. Study of â-amyloid adsorption and aggregation on graphite by STM and AFM. Chin Sci Bull, 2003, 48(5): 437–440
Qin F, Jiang Y X, Ma X Y, et al. A study of specific interaction of the transcription factor and the DNA element by atomic force microscopy. Chin Sci Bull, 2004, 49(13): 1376–1380
Allen S, Chen X Y, Davies J, et al. Detection of antigen-antibody binding envents with the atomic force microscope. Biochem, 1997, 36(24): 7457–7463
Yuan C, Chen A, Kolb P, et al. Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy. Biochem, 2000, 39(33): 10219–10223
Ros R, Schwesinger F, Anselmetti D, et al. Antigen binding forces of individually addressed single-chain Fv antibody molecules. Proc Natl Acad Sci USA, 1998, 95(13): 7402–7405
Lo Y S, Huefner N D, Chan W S, et al. Specific Interactions between biotin and avidin studied by atomic force microscopy using the Poisson statistical analysis method. Langmuir, 1999, 15(4): 1373–1382
Wong J, Chilkoti A, Moy V T. Direct force measurements of the streptavidin-biotin interaction. Biomolecular Engineering, 1999, 16(1–4): 45–55
Jiang Y X, Zhu C F, Ling L S, et al. Specific Aptamer-Protein Interaction Studied by Atomic Force Microscopy. Anal Chem, 2003, 75(9): 2112–2116
Basnar B, Elnathan R, Willner I. Following aptamer-thrombin binding by force measurements. Anal Chem, 2006, 78(11): 3638–3642
Jin Y, Wang K M, Tan W H, et al. Monitoring molecular beacon/DNA interactions using atomic force microscopy. Anal Chem, 2004, 76(19): 5721–5725
Lo Y S, Simons J, Beebe T P. Loading-rate dependence of individual ligand-receptor bond-rupture forces studied by atomic force microscopy. Langmuir, 2001, 17(12): 3741–3748
Williams J M, Han T, Beebe T P J. Determination of single-bond forces from contact force variances in atomic force microscopy. Langmuir, 1996, 12(5): 1291–1295
Stevens F, Lo Y S, Harris J M, et al. Computer modeling of atomic force microscopy force measurements: comparisons of Poisson, Histogram, and Continuum methods. Langmuir, 1999, 15(1): 207–213
Wenzler L A, Moyes G L, Olson L G, et al. Single-molecule bond-rupture force analysis of interactions between AFM tips and substrates modified with organosilanes. Anal Chem, 1997, 69(14): 2855–2861
Tian S X, Cui X Y. The investigation of human angiogenin. Chemistry of Life (in Chinese), 1996, 16(3): 25–26
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Supported by the National Key Basic Research Program (Grant No. 2002CB513100-10), Key Technologies Research and Development Program (Grant No. 2003BA310A16), Key Project Foundation of China Education Ministry (Grant No. 107084), Program for New Century Excellent Talents in University (Grant No. NCET-06-0697), National Natural Science Foundation of China (Nos. 90606003 and 20405005) and Outstanding Youth Foundation of Hunan Province (Grant No. 06JJ10004)
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He, X., Jin, R., Yang, L. et al. Study on the specific interaction between angiogenin and aptamer by atomic force microscopy (AFM). Chin. Sci. Bull. 53, 198–203 (2008). https://doi.org/10.1007/s11434-007-0494-4
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DOI: https://doi.org/10.1007/s11434-007-0494-4