Structural hysteresis and hierarchy in adsorbed glycoproteins

Journal of Chemical Physics

Volumn 129, Issue 7, 2008, Pages

  Horvath, Robert ^a   McColl, James ^a,c   Yakubov, Gleb E ^b   Ramsden, Jeremy J ^a  

^a CRANFIELD UNIVERSITY   (United Kingdom)

^b UNILEVER RESEARCH   (United Kingdom)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADSORPTION; CRYSTALLOGRAPHY; DESORPTION; ELASTICITY; HYSTERESIS; INTEGRATED OPTOELECTRONICS; MOLECULAR BEAM EPITAXY; OPTICAL MICROSCOPY; PROTEINS; SELF ASSEMBLY; THICK FILMS; THIN FILMS; VAPOR DEPOSITION;

ADSORPTION-DESORPTION; BOUNDARY LUBRICANTS; BULK CONCENTRATIONS; GENERAL FEATURE; GLYCOSYLATED; HIGH-RESOLUTION MOLECULAR MICROSCOPY; IN-SITU; LAYER THICKNESSES; MOLECULAR STATES; NANO-METER SCALE; OPTICAL WAVEGUIDE LIGHT MODE SPECTROSCOPY; SELF- ASSEMBLIES; STRUCTURAL ANISOTROPY; UNIAXIAL SYMMETRY;

GLYCOPROTEINS;

MUCIN;

ADSORPTION; ARTICLE; ARTIFICIAL MEMBRANE; CHEMISTRY; SOLUTION AND SOLUBILITY; SPECTROSCOPY; SURFACE PROPERTY; TIME;

ADSORPTION; MEMBRANES, ARTIFICIAL; MUCINS; SOLUTIONS; SPECTRUM ANALYSIS; SURFACE PROPERTIES; TIME FACTORS;

EID: 50249122120     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.2968127     Document Type: Article

References (33)

1. L. A. Blumenfeld, Problems of Biological Physics (Springer, Heidelberg, 1981).
2. J. J. Ramsden, in Complexity and Security, edited by, J. J. Ramsden, and, P. J. Kervalishvili, (IOS, Amsterdam, 2008), pp. 93-102.
3. J. Talbot, Adsorption 0929-5607 10.1007/BF00127102 2, 89 (1996).
4. J. J. Ramsden, Phys. Rev. Lett. 0031-9007 10.1103/PhysRevLett.71.295 71, 295 (1993).
5. R. Kurrat, J. J. Ramsden, and J. E. Prenosil, J. Chem. Soc., Faraday Trans. 0956-5000 10.1039/ft9949000587 90, 587 (1994).
6. R. Kurrat, J. E. Prenosil, and J. J. Ramsden, J. Colloid Interface Sci. 0021-9797 10.1006/jcis.1996.4528 185, 1 (1997).
7. P. R. Van Tassel, L. Guemouri, J. J. Ramsden, G. Tarjus, P. Viot, and J. Talbot, J. Colloid Interface Sci. 0021-9797 10.1006/jcis.1998.5781 207, 317 (1998).
8. L. Guemouri, J. Ogier, Z. Zekhnini, and J. J. Ramsden, J. Chem. Phys. 0021-9606 10.1063/1.1314861 113, 8183 (2000).
9. Ph. Roussel and Ph. Delmotte, Curr. Org. Chem. 1385-2728 10.2174/1385272043485846 8, 413 (2004).
10. R. Bansil and B. S. Turner, Curr. Opin. Colloid Interface Sci. 1359-0294 10.1016/j.cocis.2005.11.001 11, 164 (2006).
11. K. Tiefenthaler and W. Lukosz, J. Opt. Soc. Am. B 6, 209 (1989). 0740-3224
12. J. J. Ramsden, J. Stat. Phys. 0022-4715 10.1007/BF01052813 73, 853 (1993).
13. J. J. Ramsden, in Proteins at Solid-Liquid Interfaces, edited by, Ph. Dejardin, (Springer, Heidelberg, 2006), pp. 23-49.
14. J. J. Ramsden, Biopolymers 0006-3525 10.1002/bip.360330313 33, 475 (1993).
15. R. Horvath and J. J. Ramsden, Langmuir 0743-7463 10.1021/la701405n 23, 9330 (2007).
16. J. R. Lu, in Surfaces and Interfaces for Biomaterials, edited by, P. Vadgama, (Woodhead, Abington, 2005), pp. 299-321.
17. C. Viney, A. Huber, and P. Verdugo, Macromolecules 0024-9297 10.1021/ma00056a044 26, 852 (1993).
18. G. E. Yakubov, A. Papagiannopoulos, E. Rat, and T. A. Waigh, Biomacromolecules 1525-7797 10.1021/bm700721c 8, 3791 (2007).
19. G. E. Yakubov, H. -J. Butt, and O. I. Vinogradova, J. Phys. Chem. B 1089-5647 10.1021/jp000445+ 104, 3407 (2000).
20. E. K. Mann, L. Heinrich, and P. Schaaf, Langmuir 0743-7463 10.1021/la970322p 13, 4906 (1997).
21. This equation is derived by noting that it is the dielectric constants (the squares of the refractive indices) that should be averaged. Furthermore, in a uniaxial crystal two of the three axes of the index ellipsoid are equivalent.
22. This is a reasonable estimate, in accord with various measurements, made with more or less reliable assumptions, scattered in the literature. It is also in accord with rather reliable measurements of the refractive index increments of protein solutions and estimates of the mass density of adsorbed protein layers (approximately 0.6 g/ cm3).
23. W. Lukosz, Biosens. Bioelectron. 0956-5663 10.1016/S0956-5663(97)85335-3 12, 175 (1997).
24. R. Horvath, G. Fricsovszky, and E. Papp, Biosens. Bioelectron. 0956-5663 10.1016/S0956-5663(02)00154-9 18, 415 (2003).
25. Beyond a concentration of about 10% (w/w), the glycoprotein solutions become extremely viscous and difficult to manipulate experimentally.
26. A. Fernández and J. J. Ramsden, J. Biol. Phys. Chem. 1, 81 (2001).
27. J. McColl, G. E. Yakubov, and J. J. Ramsden, Langmuir 0743-7463 10.1021/la0630918 23, 7096 (2007).
28. Compare scratch tests made with an atomic force microscope, which yielded a thickness of about 4 nm.
29. G. E. Yakubov, A. Papagiannopoulos, E. Rat, R. L. Easton, and T. A. Waigh, Biomacromolecules 8, 3467 (2007).
30. V. Ball and J. J. Ramsden, Biopolymers 46, 489 (1998).
31. For all practical purposes, i.e., within the experimental uncertainty of the measurement, the M thus calculated is the same as that obtained by substituting 〈 nA 〉 and dA in Eq. by the unrealistic refractive index and thickness calculated from the homogeneous and isotropic analysis (cf. Ref.).
32. O. Wiener, Abh. math.-phys. Kl. königl. sächs. Ges.-Wiss. 32, 503 (1912).
33. Atomic force microscopy carried out at this point reveals holes in the protein layer.