Abstract
The effect of the properties of a protein on its adsorption to a metal surface in the presence of external electric potential was investigated. Protein adsorption processes at different surface potentials were measured for fifteen types of proteins using an in-situ ellipsometry. The tested proteins were classified into three groups, based on the amount of protein that was adsorbed as a function of the surface potential: In First group of proteins, an increasing trend for the amount adsorbed with a more positive surface potential was found; The amount adsorbed of α-chymotrypsinogen A and ribonuclease A (Second group) were roughly constant and independent of the applied surface electric potentials; In Third group, the amount adsorbed decreased with increasing surface potential. This protein classification was correlated with the isoelectric points of the proteins (First group: ≤9.3; Second group: 9.3–10; Third group: >10). Increasing the pH positively and negatively shifted the surface potentials, allowing ß-lactoglobulin (First group) and lysozyme (Third) to become adsorbed, respectively. The surface potential range for protein adsorption was also markedly shifted depending on the metal substrate type. These findings were interpreted based on the electrostatic interactions among the protein, surface hydroxyl groups, and the applied external electric field.
| Original language | English |
|---|---|
| Pages (from-to) | 262-268 |
| Number of pages | 7 |
| Journal | Colloids and Surfaces B: Biointerfaces |
| Volume | 166 |
| DOIs | |
| Publication status | Published - Jun 1 2018 |
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Keywords
- Electrostatic interaction
- Ellipsometer
- External electric potential
- Isoelectric point
- Metal oxide surface
- Protein adsorption
- Surface hydroxyl group
ASJC Scopus subject areas
- Biotechnology
- Surfaces and Interfaces
- Physical and Theoretical Chemistry
- Colloid and Surface Chemistry
Cite this
Adsorption characteristics of various proteins on a metal surface in the presence of an external electric potential. / Htwe, Ei Ei; Nakama, Yuhi; Yamamoto, Yuko; Tanaka, Hiroshi; Imanaka, Hiroyuki; Ishida, Naoyuki; Imamura, Koreyoshi.
In: Colloids and Surfaces B: Biointerfaces, Vol. 166, 01.06.2018, p. 262-268.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Adsorption characteristics of various proteins on a metal surface in the presence of an external electric potential
AU - Htwe, Ei Ei
AU - Nakama, Yuhi
AU - Yamamoto, Yuko
AU - Tanaka, Hiroshi
AU - Imanaka, Hiroyuki
AU - Ishida, Naoyuki
AU - Imamura, Koreyoshi
PY - 2018/6/1
Y1 - 2018/6/1
N2 - The effect of the properties of a protein on its adsorption to a metal surface in the presence of external electric potential was investigated. Protein adsorption processes at different surface potentials were measured for fifteen types of proteins using an in-situ ellipsometry. The tested proteins were classified into three groups, based on the amount of protein that was adsorbed as a function of the surface potential: In First group of proteins, an increasing trend for the amount adsorbed with a more positive surface potential was found; The amount adsorbed of α-chymotrypsinogen A and ribonuclease A (Second group) were roughly constant and independent of the applied surface electric potentials; In Third group, the amount adsorbed decreased with increasing surface potential. This protein classification was correlated with the isoelectric points of the proteins (First group: ≤9.3; Second group: 9.3–10; Third group: >10). Increasing the pH positively and negatively shifted the surface potentials, allowing ß-lactoglobulin (First group) and lysozyme (Third) to become adsorbed, respectively. The surface potential range for protein adsorption was also markedly shifted depending on the metal substrate type. These findings were interpreted based on the electrostatic interactions among the protein, surface hydroxyl groups, and the applied external electric field.
AB - The effect of the properties of a protein on its adsorption to a metal surface in the presence of external electric potential was investigated. Protein adsorption processes at different surface potentials were measured for fifteen types of proteins using an in-situ ellipsometry. The tested proteins were classified into three groups, based on the amount of protein that was adsorbed as a function of the surface potential: In First group of proteins, an increasing trend for the amount adsorbed with a more positive surface potential was found; The amount adsorbed of α-chymotrypsinogen A and ribonuclease A (Second group) were roughly constant and independent of the applied surface electric potentials; In Third group, the amount adsorbed decreased with increasing surface potential. This protein classification was correlated with the isoelectric points of the proteins (First group: ≤9.3; Second group: 9.3–10; Third group: >10). Increasing the pH positively and negatively shifted the surface potentials, allowing ß-lactoglobulin (First group) and lysozyme (Third) to become adsorbed, respectively. The surface potential range for protein adsorption was also markedly shifted depending on the metal substrate type. These findings were interpreted based on the electrostatic interactions among the protein, surface hydroxyl groups, and the applied external electric field.
KW - Electrostatic interaction
KW - Ellipsometer
KW - External electric potential
KW - Isoelectric point
KW - Metal oxide surface
KW - Protein adsorption
KW - Surface hydroxyl group
UR - http://www.scopus.com/inward/record.url?scp=85044507142&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85044507142&partnerID=8YFLogxK
U2 - 10.1016/j.colsurfb.2018.03.035
DO - 10.1016/j.colsurfb.2018.03.035
M3 - Article
C2 - 29604568
AN - SCOPUS:85044507142
VL - 166
SP - 262
EP - 268
JO - Colloids and Surfaces B: Biointerfaces
JF - Colloids and Surfaces B: Biointerfaces
SN - 0927-7765
ER -