In situ characterization of the adsorbed concanavalin A on germanium surface at various pH

Biotechnology Progress

Volumn 24, Issue 4, 2008, Pages 972-980

  Dong, Jie ^a,b   Mielczarski, Jerzy A ^a   Mielczarski, Ela ^a   Xu, Zhenghe ^a,b  

^a UNIVERSITÉ DE LORRAINE   (France)

^b UNIVERSITY OF ALBERTA   (Canada)

Author keywords

Adsorption models; Adsorption desorption; ATR infrared; Concanavalin A; In situ characterization

Indexed keywords

ADSORPTION; ELECTROLYTES; FLOW INTERACTIONS; GAS ADSORPTION; GERMANIUM; HYDRATION; HYDROGEN; HYDROGEN BONDS; HYDROPHOBICITY; INFRARED SPECTROSCOPY; NONMETALS; PARAMETER ESTIMATION; PHYSISORPTION;

ADSORBED LAYERS; ADSORPTION MODELS; ADSORPTION PROCESSES; ADSORPTION/DESORPTION; ATR INFRARED; ATTENUATED TOTAL REFLECTION INFRARED SPECTROSCOPY; CONCANAVALIN A; ELECTROL YTE SOLUTIONS; EXPERIMENTAL METHODOLOGY; EXPERIMENTAL SPECTRA; GERMANIUM SUBSTRATES; GERMANIUM SURFACE; HYDRATION LEVEL; HYDROGEN BONDINGS; HYDROPHOBIC INTERACTIONS; IN SITU CHARACTERIZATION; IN-SITU; MONOLAYER COVERAGE; NATIVE OXIDES; PH CHANGES; PH-DEPENDENT; PHOSPHATE-BUFFERED SALINE; PROTEIN COATINGS; PROTEIN LAYERS; PROTEIN-PROTEIN INTERACTION; QUANTITATIVE EVALUATION; SIMULATED SPECTRUM; SPECTRAL SIMULATIONS; SURFACE LAYERING; VARIOUS PH;

QUALITY CONTROL;

CONCANAVALIN A; GERMANIUM;

ADSORPTION; CHEMISTRY; CONFERENCE PAPER; INFRARED SPECTROPHOTOMETRY; KINETICS; PH; SURFACE PROPERTY;

ADSORPTION; CONCANAVALIN A; GERMANIUM; HYDROGEN-ION CONCENTRATION; KINETICS; SPECTROPHOTOMETRY, INFRARED; SURFACE PROPERTIES;

EID: 51849092529     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1002/btpr.2     Document Type: Conference Paper

References (53)

1. Horbett TA, Brash JL, editors. Proteins at Interfaces. II. Fundamentals and Applications. Washington, DC: American Chemical Society; 1995.
2. Brash JL, Horbett TA, editors. Proteins at Interfaces: Physicochemical and Biochemical Studies. Washington, DC: American Chemical Society; 1987.
3. Andrade JD, Hlady V. Protein adsorption and materials biocompatibility: a tutorial review and suggested hypotheses. Adv Polym Sci. 1986;79:1-63.
4. Sandu C, Singh RK. Energy increase in operation and cleaning due to hear-exchanger fouling in milk. Food Technol. 1991;45;84-91.
5. Hubbell JA. Biomaterials in tissue engineering. Bio-Technology. 1995;13:565-576.
6. Ishihara K, Oshida H, Endo Y, Ueda T, Watanabe A, Nakabayashi N. Hemocompatibility of human whole blood on polymers with a phospholipid polar group and its mechanism. J Biomed Mater Res. 1992;26:1543-1552.
7. Feng M, Morales, AB, Beugeling T, Bantjes A, Vanderwerf K, Gosselink G, Degrooth B, Greve J. Adsorption of high density lipoproteins (HDL) on solid surfaces. J Colloid Interface Sci. 1996;177:364-371.
8. Martin BD, Gaber BP, Patterson CH, Turner DC. Direct protein microarray fabrication using a hydrogel "stamper". Langmuir. 1998;14:3971-3975.
9. Inglis W, Sanders GHW, Williams PM, Davies MC, Roberts CJ, Tendler SJB. A simple method for biocompatible polymer based spatially controlled adsorption of blood plasma proteins to a surface. Langmuir. 2001;17:7402-7405.
10. Klibanov AM. Immobilized enzymes and cells as practical catalysts. Science. 1983;219:722-727.
11. Haynes CA, Norde W. Globular proteins at solid/liquid interfaces. Colloid Surf B. 1994;2:517-566.
12. Ball A, Jones RAL. Conformational changes in adsorbed proteins. Langmuir. 1995;11:3542-3548.
13. Ishiguro R, Yokoyama Y, Maeda H, Shimamura A, Kameyama K, Hiramatsu K. Modes of conformational changes of proteins adsorbed on a planar hydrophobic polymer surface reflecting their adsorption behaviors. J Colloid Interface Sci. 2005;290:91-101.
14. Sharon N, Lis H. Lectins: cell-agglutinating and sugar-specific proteins. Science. 1972;177:949-959.
15. Fink AL, Calciano LJ, Goto Y, Kurotsu T, Palleros DR. Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry. 1994;33:12504-12511.
16. Revell DJ, Knight JR, Blyth DJ, Haines AH, Russell DA. Self-assembled carbohydrate monolayers: formation and surface selective molecular recognition. Langmuir. 1998;14:4517-4524.
17. Gestwicki JE, Strong LE, Cairo, CW, Bohem FJ, Kiessling LL. Cell aggregation by scaffolded receptor clusters. Chem Biol. 2002;9:163-169.
18. Clark A, Denborough M. The interaction of Concanavalin A with blood-group-substance glycoproteins from human seretions. Biochem J. 1971;121:811-816.
19. Kornfeld R, Ferris C. Interaction of immunoglobulin glycopeptides with Concanavalin A. J Biol Chem. 1975;250:2614-2619.
20. Brattain M, Jones C, Pittman J, Pretlow T. The purification of carcinoembryonic antigen by glutaraldehyde cross-linked Concanavalin A. Biochem Biophys Res Commun. 1975;65:63-67.
21. Boenisch T, Norgaard-Pedersen B. Carcinoembryonic antigen (CEA) of human tissue extracts: partial characterization of two variants separated by affinity chromatography on Concanavalin A. Clin Chim Acta. 1975;60:25-32.
22. Harmony J, Cordes E. Interaction of human plasma low density lipoprotein with Concanavalin A and with Ricin. J Biol Chem. 1975;250:8614-8617.
23. Picken R, Beachman I. The interaction of Concanavalin A with mutant and wild-type strain of Escherichia coli K12. Biochem Soc Trans. 1975;3:387-388.
24. Brunson K, Watson D. Concanavalin A preparation with activities related to bacterial lipopolysaccharide. J Immunol. 1975;115:599-600.
25. Shoham J, Inbar M, Sachs L. Differential toxicity on normal and transformed cells in vitro and inhibition of tumour development in vitro by Concanavalin A. Nature. 1970;227:1244-1246.
26. Inbar M, Sachs L. Structural difference in sites on the surface membrane of normal and transformed cells. Nature. 1969;223:710-712.
27. Tsuruo T, Yamori T, Tsukagoshi S, Sakurai Y. Enhanced cytocidal action of methotrexate by conjugation to Concanavalin A. Int J Cancer. 1980;26:655-659.
28. Lebed K, Pyka-Fosciak G, Raczkowska J, Lekka M, Styczeń, J. Binding activity of patterned Concanavalin A studied by atomic force microscopy. J Phys: Condens Matter. 2005;17:S1447-S1458.
29. Heng Z, Snyder M. Protein chip technology. Curr Opin Chem Biol. 2003;7:55-63.
30. Mielczarski JA, Dong J, Mielczarski E. Real time qualitative and quantitative evaluations of the adsorption of Concanavalin A on polystyrene. J Phys Chem B. 2008;112:5228-5237.
31. Su TJ, Lu JR, Thomas RK, Cui ZF, Penfold J. The effect of solution pH on the structure of lysozyme layers adsorbed at the silica-water interface studied by neutron reflection. Langmuir. 1998;14:438-445.
32. Shoham M, Yonath A, Sussman JL, Moult J, Traub W, Kalb AJ. Crystal structure of demetallized concanavalin A: the metalbinding region. J Mol Biol. 1979;131:137-155.
33. McCubbin WD, Kay CM. Molecular weight studies on concanavalin A. Biochem Biophys Res Commun. 1971;44:101-109.
34. Bouckaert J, Loris R, Poortmans F, Wyns L. Crystallographic structure of metal-free concanavalin A at 2.5 Å resolution. Proteins Struct Funct Genet. 1995;23:510-524.
35. Morita M, Ohmi T, Hasegawa E, Kawakami M, Ohwada M. Growth of native oxide on a silicon surface. J Appl Phys. 1990;68:1272-1281.
36. Palik ED. Handbook of Optical Constants of Solids. Washington, DC: Naval Research Laboratory, Academic Press; 1985.
37. Downing HD, Williams D. Optical-constants of water in infrared. J Geophys Res. 1975;80:1656-1661.
38. Mielczarski JA, Milosevic M, Berets SL. Optical properties of strongly absorbing media determined by external reflection spectroscopy. Appl Spectrosc. 1992;46:1040-1044.
39. Hansen WN. Electric fields produced by the propagation of plane coherent electromagnetic radiation in a stratified medium. J Opt Soc Am. 1968;58:380-390.
40. Harrick NJ. Internal Reflection Spectroscopy, 3rd ed. Ossining, New York: Harrick Scientific; 1987.
41. Mielczarski JA, Yoon RH. Fourier transform infrared external reflection study of molecular orientation in spontaneously adsorbed layers on low-absorption substrate. J Phys Chem. 1989;93:2034-2038.
42. Mielczarski JA, Yoon RH. Spectroscopic studies of the structure of the adsorption layer of thionocarbamate. Part 2: On cuprous sulfide. Langmuir. 1991;7:101-108.
43. Mielczarski JA. External reflection infrared spectroscopy at metallic, semiconductor, and nonmetallic substrates. Part 1: Monolayer films. J Phys Chem. 1993;97:2649-2643.
44. Mielczarski JA, Mielczarski E. Determination of molecular orientation and thickness of self-assembled monolayers of oleate on apatite by FTIR reflection spectroscopy. J Phys Chem. 1995;99:3206-3217.
45. Mielczarski JA, Mielczarski E, Zachwieja J, Cases JM. In situ and ex situ infrared studies of nature and structure of thiol monolayers adsorbed on cuprous sulfide at controlled potential. Langmuir. 1995;11:2787-2799.
46. Mielczarski E, Mielczarski JA, Cases JM. Molecular recognition effect in monolayer formation of oleate on fluorite. Langmuir. 1998;14:1739-1747.
47. Mielczarski JA, Mielczarski E, Cases JM. Dynamics of fluoriteoleate interactions. Langmuir. 1999;15:500-508.
48. Mielczarski JA, Mielczarski E. Infrared external reflection spectroscopy of adsorbed monolayers in a region of strong absorption of substrate. J Phys Chem B. 1999;103:5852-5859.
49. Mielczarski E, Duval YB, Mielczarski JA. Spectroscopic characterization of the nature and structure of adsorbed organic monolayers on quartz in the region of very strong absorption of Substrate. Reverse surface selection rule. J Phys Chem B. 2002;106:11985-11992.
50. Lahiri J, Isaacs L, Tien J, Whitesides GM. A strategy for the generation of surfaces presenting ligands for studies of binding based on an active ester as a common reactive intermediate: a surface plasmon resonance study. Anal Chem. 1999;71:777-790.
51. Hardman KD, Ainsworth CF. Structure of concanavalin A at 2.4-Å resolution. Biochemistry. 1972;11:4910-4919.
52. Einspahr H, Parks EH, Suguna K, Subramanian E, Suddath FL. The crystal structure of pea lectin at 3.0-Å resolution. J Biol Chem. 1986;261:16518-16527.
53. Loris R, Hamelryck T, Bouckaert J, Wyns L. Legume lectin structure. Biochimica et Biophysica Acta-Prot Struct Mol Enzymol. 1998;1383:9-36.