| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Biophysical Journal 70: 2052-2066 (1996)
© 1996 the Biophysical Society
Department of Biochemistry, Swiss Federal Institute of Technology, ETH Zentrum, Zurich, Switzerland. pwagner@cmgm.stanford.edu
ABSTRACT
We have worked out a procedure for covalent binding of native biomacromolecules on flat gold surfaces for scanning probe microscopy in aqueous buffer solutions and for other nanotechnological applications, such as the direct measurement of interaction forces between immobilized macromolecules, of their elastomechanical properties, etc. It is based on the covalent immobilization of amino group-containing biomolecules (e.g., proteins, phospholipids) onto atomically flat gold surfaces via omega-functionalized self-assembled monolayers. We present the synthesis of the parent compound, dithio-bis(succinimidylundecanoate) (DSU), and a detailed study of the chemical and physical properties of the monolayer it forms spontaneously on Au(111). Scanning tunneling microscopy and atomic force microscopy (AFM) revealed a monolayer arrangement with the well-known depressions that are known to stem from an etch process during the self-assembly. The total density of the omega-N-hydroxysuccinimidyl groups on atomically flat gold was 585 pmol/cm(2), as determined by chemisorption of (14)C-labeled DSU. This corresponded to approximately 75% of the maximum density of the omega-unsubstituted alkanethiol. Measurements of the kinetics of monolayer formation showed a very fast initial phase, with total coverage within 30 S. A subsequent slower rearrangement of the chemisorbed molecules, as indicated by AFM, led to a decrease in the number of monolayer depressions in approximately 60 min. The rate of hydrolysis of the omega-N-hydroxysuccinimide groups at the monolayer/water interface was found to be very slow, even at moderately alkaline pH values. Furthermore, the binding of low-molecular-weight amines and of a model protein was investigated in detail.
This article has been cited by other articles:
 |
|
 |
|
  B. J. Yakes, R. J. Lipert, J. P. Bannantine, and M. D. Porter Impact of Protein Shedding on Detection of Mycobacterium avium subsp. paratuberculosis by a Whole-Cell Immunoassay Incorporating Surface-Enhanced Raman Scattering Clin. Vaccine Immunol., February 1, 2008; 15(2): 235 - 242. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Backmann, C. Zahnd, F. Huber, A. Bietsch, A. Pluckthun, H.-P. Lang, H.-J. Guntherodt, M. Hegner, and C. Gerber A label-free immunosensor array using single-chain antibody fragments PNAS, October 11, 2005; 102(41): 14587 - 14592. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M Berry, D Brayshaw, and T J McMaster Dynamic molecular resolution imaging of preocular fluid impressions Br. J. Ophthalmol., November 1, 2004; 88(11): 1460 - 1466. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. L. Huff, M. P. Lynch, S. Nettikadan, J. C. Johnson, S. Vengasandra, and E. Henderson Label-Free Protein and Pathogen Detection Using the Atomic Force Microscope J Biomol Screen, September 1, 2004; 9(6): 491 - 497. [Abstract] [PDF]
|
|
|
|
|
|
G.-Y. Liu and N. A. Amro Supramolecular Chemistry And Self-assembly Special Feature: Positioning protein molecules on surfaces: A nanoengineering approach to supramolecular chemistry PNAS, April 16, 2002; 99(8): 5165 - 5170. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. A. Ruiz-Taylor, T. L. Martin, F. G. Zaugg, K. Witte, P. Indermuhle, S. Nock, and P. Wagner Monolayers of derivatized poly(L-lysine)-grafted poly(ethylene glycol) on metal oxides as a class of biomolecular interfaces PNAS, January 30, 2001; 98(3): 852 - 857. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
