Abstract
Protein adsorption at the liquid-solid interface is critically important for the development of biomedical materials. Surface plasmon resonance (SPR) has been widely used in real-time monitoring of protein adsorption behavior on surfaces. However, the number of combinations of protein-surface interactions that can be measured in a single experiment is limited by a conventional SPR apparatus. We assembled an SPR imaging apparatus for high-throughput studies of many sets of protein-surface interactions. In addition, SPR sensor surfaces with arrayed spots carrying different surface properties were prepared by taking advantage of self-assembled monolayers of alkanethiols. The combination of the SPR imaging apparatus and the arrayed sensor surfaces allows for multiple and real-time monitoring of protein-surface interactions.
| Original language | English |
|---|---|
| Title of host publication | Proteins at Interfaces III State of the Art |
| Publisher | American Chemical Society |
| Pages | 695-708 |
| Number of pages | 14 |
| ISBN (Print) | 9780841227965 |
| DOIs | |
| Publication status | Published - Dec 12 2012 |
| Externally published | Yes |
Publication series
| Name | ACS Symposium Series |
|---|---|
| Volume | 1120 |
| ISSN (Print) | 0097-6156 |
| ISSN (Electronic) | 1947-5918 |
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All Science Journal Classification (ASJC) codes
- Chemistry(all)
- Chemical Engineering(all)
Cite this
High-throughput study of protein-surface interactions using a surface plasmon resonance imaging apparatus. / Arima, Yusuke; Ishii, Rika; Hirata, Isao; Iwata, Hiroo.
Proteins at Interfaces III State of the Art. American Chemical Society, 2012. p. 695-708 (ACS Symposium Series; Vol. 1120).Research output: Chapter in Book/Report/Conference proceeding › Conference contribution
}
TY - GEN
T1 - High-throughput study of protein-surface interactions using a surface plasmon resonance imaging apparatus
AU - Arima, Yusuke
AU - Ishii, Rika
AU - Hirata, Isao
AU - Iwata, Hiroo
PY - 2012/12/12
Y1 - 2012/12/12
N2 - Protein adsorption at the liquid-solid interface is critically important for the development of biomedical materials. Surface plasmon resonance (SPR) has been widely used in real-time monitoring of protein adsorption behavior on surfaces. However, the number of combinations of protein-surface interactions that can be measured in a single experiment is limited by a conventional SPR apparatus. We assembled an SPR imaging apparatus for high-throughput studies of many sets of protein-surface interactions. In addition, SPR sensor surfaces with arrayed spots carrying different surface properties were prepared by taking advantage of self-assembled monolayers of alkanethiols. The combination of the SPR imaging apparatus and the arrayed sensor surfaces allows for multiple and real-time monitoring of protein-surface interactions.
AB - Protein adsorption at the liquid-solid interface is critically important for the development of biomedical materials. Surface plasmon resonance (SPR) has been widely used in real-time monitoring of protein adsorption behavior on surfaces. However, the number of combinations of protein-surface interactions that can be measured in a single experiment is limited by a conventional SPR apparatus. We assembled an SPR imaging apparatus for high-throughput studies of many sets of protein-surface interactions. In addition, SPR sensor surfaces with arrayed spots carrying different surface properties were prepared by taking advantage of self-assembled monolayers of alkanethiols. The combination of the SPR imaging apparatus and the arrayed sensor surfaces allows for multiple and real-time monitoring of protein-surface interactions.
UR - http://www.scopus.com/inward/record.url?scp=84905014747&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84905014747&partnerID=8YFLogxK
U2 - 10.1021/bk-2012-1120.ch032
DO - 10.1021/bk-2012-1120.ch032
M3 - Conference contribution
AN - SCOPUS:84905014747
SN - 9780841227965
T3 - ACS Symposium Series
SP - 695
EP - 708
BT - Proteins at Interfaces III State of the Art
PB - American Chemical Society
ER -