TY - JOUR
T1 - Voltammetric evaluation of lectin-sugar binding at a mannose/thionine- modified Au electrode
AU - Sugawara, Kazuharu
AU - Shirotori, Tatsuya
AU - Hirabayashi, George
AU - Kuramitz, Hideki
AU - Tanaka, Shunitz
N1 - Funding Information:
The authors thank the Ministry of Education, Culture, Sports, Science and Technology of Japan for support of this work under a Grant-in-Aid for Scientific Research (No. 09740548).
PY - 2004/7/1
Y1 - 2004/7/1
N2 - To evaluate lectin-sugar interactions, a sugar/thionine-modified Au electrode was constructed. In this study, concanavalin A(Con A)-mannose binding at a mannose/thionine-modified electrode was investigated with voltammetry. Thionine with two active amino groups was selected as an electroactive compound. One amino group combines with 3,3′-dithiobis (sulfosuccinimidyl propionate), and the other amino group combines with sugar. Because the prepared reagent has a disulfide group, the Au electrode is modified with a self-assembled multilayer. When Con A-mannose binding at the electrode occurred, the thionine moiety was held at the binding site of Con A to mannose. Therefore, the binding was monitored through the decrease of the electrode response of the thionine moiety. On the other hand, measurements to several lectins not having binding sites to mannose were carried out. In the presence of Con A, measurement at a galactose/thionine-modified electrode was also attempted. As a result, almost no decrease of the peak current was observed. Consequently, it is concluded that the mannose/thionine-modified Au electrode responds selectively to Con A.
AB - To evaluate lectin-sugar interactions, a sugar/thionine-modified Au electrode was constructed. In this study, concanavalin A(Con A)-mannose binding at a mannose/thionine-modified electrode was investigated with voltammetry. Thionine with two active amino groups was selected as an electroactive compound. One amino group combines with 3,3′-dithiobis (sulfosuccinimidyl propionate), and the other amino group combines with sugar. Because the prepared reagent has a disulfide group, the Au electrode is modified with a self-assembled multilayer. When Con A-mannose binding at the electrode occurred, the thionine moiety was held at the binding site of Con A to mannose. Therefore, the binding was monitored through the decrease of the electrode response of the thionine moiety. On the other hand, measurements to several lectins not having binding sites to mannose were carried out. In the presence of Con A, measurement at a galactose/thionine-modified electrode was also attempted. As a result, almost no decrease of the peak current was observed. Consequently, it is concluded that the mannose/thionine-modified Au electrode responds selectively to Con A.
KW - Lectin
KW - SAM
KW - Sugar
KW - Thionine
UR - http://www.scopus.com/inward/record.url?scp=2442641695&partnerID=8YFLogxK
U2 - 10.1016/j.jelechem.2003.12.015
DO - 10.1016/j.jelechem.2003.12.015
M3 - 学術論文
AN - SCOPUS:2442641695
SN - 1572-6657
VL - 568
SP - 7
EP - 12
JO - Journal of Electroanalytical Chemistry
JF - Journal of Electroanalytical Chemistry
IS - 1-2
ER -