Abstract
We report on the use of PDMS multichannels for affinity studies of DNA aptamer–human Immunoglobulin E (IgE) interactions by surface plasmon resonance imaging (SPRi). The sensing surface was prepared with thiol-terminated aptamers through a self-assembling process in the PDMS channels defined on a gold substrate. Cysteamine was codeposited with the thiol aptamers to promote proper spatial arrangement of the aptamers and thus maintain their optimal binding efficiencies. Four aptamers with different nucleic acid sequences were studied to test their interaction affinity toward IgE, and the results confirmed that aptamer I (5′-SH-GGG GCA CGT TTA TCC GTC CCT CCT AGT GGC GTG CCC C-3′) has the strongest binding affinity. Control experiments were conducted with a PEG-functionalized surface and IgG was used to replace IgE in order to verify the selective binding of aptamer I to the IgE molecules. A linear concentration-dependent relationship between IgE and aptamer I was obtained, and a 2-nM detection limit was achieved. SPRi data were further analyzed by global fitting, and the dissociation constant of aptamer I–IgE complex was found to be 2.7 × 10−7 M, which agrees relatively well with the values reported in the literature. Aptamer affinity screening by SPR imaging demonstrates marked advantages over competing methods because it does not require labeling, can be used in real-time, and is potentially high-throughput. The ability to provide both qualitative and quantitative results on a multichannel chip further establishes SPRi as a powerful tool for the study of biological interactions in a multiplexed format.
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References
Hermann T, Patel DJ (2000) Science 287:820–825
Bock LC, Griffin LC, Latham JA, Vermaas EH, Toole JJ (1992) Nature 355:564–566
Shi H, Hoffman BE, Lis JT (1999) Proc Natl Acad Sci USA 96:10033–10038
Gold L, Polisky B, Uhlenbeck O, Yarus M (1995) Ann Rev Biochem 64:763–797
Tombelli S, Minunni A, Mascini A (2005) Biosens Bioelectron 20:2424–2434
Liu HX, Zhang M, Krainer AR (1998) Genes Dev 12:1998–2012
Wilson DS, Szostak JW (1999) Ann Rev Biochem 68:611–647
Li JWJ, Fang XH, Schuster SM, Tan WH (2000) Angew Chem Int Edit 39:1049–1052
O’Sullivan CK (2002) Anal Bioanal Chem 372:44–48
Hamaguchi N, Ellington A, Stanton M (2001) Anal Biochem 294:126–131
Li JWJ, Fang XH, Tan WH (2002) Mol Cell Biol Res Commun 292:31–40
McCauley TG, Hamaguchi N, Stanton M (2003) Anal Biochem 319:244–250
Nelson BP, Grimsrud TE, Liles MR, Goodman RM, Corn RM (2001) Anal Chem 73:1–7
Shumaker-Parry JS, Aebersold R, Campbell CT (2004) Anal Chem 76:2071–2082
Xu DK, Xu DW, Yu XB, Liu ZH, He W, Ma ZQ (2005) Anal Chem 77:5107–5113
Kanda V, Kariuki JK, Harrison DJ, McDermott MT (2004) Anal Chem 76:7257–7262
Liss M, Petersen B, Wolf H, Prohaska E (2002) Anal Chem 74:4488–4495
Kikuchi K, Umehara T, Fukuda K, Hwang J, Kuno A, Hasegawa T, Nishikawa S (2003) J Biochem 133:263–270
Surugiu-Warnmark I, Warnmark A, Toresson G, Gustafsson JA, Bulow L (2005) Mol Cell Biol Res Commun 332:512–517
Dey AK, Griffiths C, Lea SM, James W (2005) RNA 11:873–884
Tombelli S, Minunni A, Luzi E, Mascini M (2005) Bioelectrochemistry 67:135–141
Rich RL, Myszka DG (2000) Curr Opin Biotechnol 11:54–61
Rich RL, Day YSN, Morton TA, Myszka DG (2001) Anal Biochem 296 197–207
Yoshida T, Sato M, Ozawa T, Umezawa Y (2000) Anal Chem 72:6–11
Wink T, van Zuilen SJ, Bult A, van Bennekom WP (1998) Anal Chem 70:827–832
Brockman JM, Nelson BP, Corn RM (2000) Annu Rev Phys Chem 51:41–63
Brockman JM, Frutos AG, Corn RM (1999) J Am Chem Soc 121:8044–8051
Shumaker-Parry JS, Zareie MH, Aebersold R, Campbell CT (2004) Anal Chem 76:918–929
Wolf LK, Fullenkamp DE, Georgiadis RM (2005) J Am Chem Soc 127 17453–17459
Wilkop T, Wang ZZ, Cheng Q (2004) Langmuir 20:11141–11148
Kanda V, Kitov P, Bundle DR, McDermott MT (2005) Anal Chem 77:7497–7504
Jung SO, Ro HS, Kho BH, Shin YB, Kim MG, Chung BH (2005) Proteomics 5:4427–4431
Kim M, Park K, Jeong EJ, Shin YB, Chung BH (2006) Anal Biochem 351:298–304
Kanoh N, Kyo M, Inamori K, Ando A, Asami A, Nakao A, Osada H (2006) Anal Chem 78:2226–2230
Lee HJ, Yan YL, Marriott G, Corn RM (2005) J Physiol–Lond 563:61–71
Nakamura F, Ito M, Manna A, Tamada K, Hara M, Knoll W (2006) Jap J Appl Phys Pt 1 45:1026–1029
Okumura A, Sato Y, Kyo M, Kawaguchi H (2005) Anal Biochem 339:328–337
Ro HS, Koh BH, Jung SO, Park HK, Shin YB, Kim MG, Chung BH (2006) Proteomics 6:2108–2111
Smith EA, Thomas WD, Kiessling LL, Corn RM (2003) J Am Chem Soc 125:6140–6148
Lee HJ, Wark AW, Goodrich TT, Fang SP, Corn RM (2005) Langmuir 21:4050–4057
Phillips KS, Cheng Q (2005) Anal Chem 77:327–334
Wang ZZ, Wilkop T, Cheng Q (2005) Langmuir 21:10292–10296
Goss CA, Charych DH, Majda M (1991) Anal Chem 63:85–88
Rich RL, Myszka DG (2000) J Mol Recognit 13:388–407
Baird CL, Myszka DG (2001) J Mol Recognit 14 261–268
Morton TA, Myszka DG, Chaiken IM (1995) Anal Biochem 227:176–185
Myszka DG, Arulanantham PR, Sana T, Wu ZN, Morton TA, Ciardelli TL (1996) Protein Sci 5:2468–2478
Wiegand TW, Williams PB, Dreskin SC, Jouvin MH, Kinet JP, Tasset D (1996) J Immunol 157:221–230
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This work was supported in part by the National Science Foundation (BES-0428908).
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Wang, Z., Wilkop, T., Xu, D. et al. Surface plasmon resonance imaging for affinity analysis of aptamer–protein interactions with PDMS microfluidic chips. Anal Bioanal Chem 389, 819–825 (2007). https://doi.org/10.1007/s00216-007-1510-x
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DOI: https://doi.org/10.1007/s00216-007-1510-x