Direct Observation of Self-Assembled Monolayers, Ion Complexation, and Protein Conformation at the Gold/Water Interface: An FTIR Spectroscopic Approach
Source abstract
Abstract
A simple approach to the in situ measurement of infrared spectra of self-assembled monolayers (SAMs) on gold in an aqueous environment is described. A thin gold film (3−5 nm) on the surface of a germanium internal reflection element is used as a substrate for the self-assembly of a monolayer of a chelating thioalkane. High signal-to-noise spectra are obtained, allowing identification of the chemical groups present in the SAM. Complexation of ions by the SAM can be monitored, and the secondary conformation of his-tagged proteins bound to the SAM can be observed.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Lipid Membrane Structure and Behavior · Molecular Junctions and Nanostructures · Spectroscopy and Quantum Chemical Studies
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Laboratoire de Chimie Physique des Polymères et Membranes, Swiss Federal Institute of Technology Lausanne, CH-1015 Ecublens, Switzerland
References (19)
Show source-provided references
1. Prime K. L. · Science · 1991 · 252 · 116410.1126/science.252.5009.1164 ↗
2. Terrettaz S. · Langmuir · 1993 · 9 · 136110.1021/la00029a033 ↗
3. Plant A. L. · Biophys. J. · 1994 · 67 · 112610.1016/S0006-3495(94)80579-X ↗
4. Spinke J. · Langmuir · 1993 · 9 · 182110.1021/la00031a033 ↗
5. DiMilla P. A. · J. Am. Chem. Soc. · 1994 · 116 · 222510.1021/ja00084a105 ↗
6. From the optical constants of bulk gold in the IR, we calculate the exponential decay length of an IR wave in gold at around 1700 cm-1(6 μm) to be approximately 28 nm.
7. Harrick N. J. · 1967
8. Hatta A. · Appl. Surf. Sci. · 1986 · 25 · 32710.1016/0169-4332(86)90064-4 ↗
9. Porath J. · Nature · 1975 · 258 · 59810.1038/258598a0 ↗
10. Hochuli · 1990 · 12 · 8710.1007/978-1-4613-0641-2_6 ↗
11. Keller T. A. · Supramol. Sci. · 1995 · 2 · 15510.1016/0968-5677(96)89670-2 ↗
12. Sigal G. B. · Anal. Chem. · 1996 · 68 · 49010.1021/ac9504023 ↗
13. Schmitt L. · Angew. Chem., Int. Ed. Engl. · 1996 · 35 · 31710.1002/anie.199603171 ↗
14. Tomita Y. · Bull. Chem. Soc. Jpn. · 1963 · 36 · 106910.1246/bcsj.36.1069 ↗
15. Nakamoto K. · J. Am. Chem. Soc. · 1962 · 84 · 208110.1021/ja00870a016 ↗
16. Goormaghtigh, E.; Cabiaux, V.; Ruysschaert, J.M. InSubcellularBiochemistry; Hilderson, H. J., Ralston, G. B., Eds.; Plenum Press: New York, 1994; Vol. 23, p 329.10.1007/978-1-4615-1863-1_8 ↗
17. Byler D. M. · Biopolymers · 1986 · 25 · 46910.1002/bip.360250307 ↗
18. Buijs J. · Langmuir · 1996 · 12 · 160510.1021/la950665s ↗
19. Seki H. · IBM J. Res. Dev. · 1993 · 37 · 22710.1147/rd.372.0227 ↗