TY - JOUR
T1 - Observation of photoactive yellow protein anchored to a modified Au(1 1 1) surface by scanning tunneling microscopy
AU - Rzeźnicka, Izabela I.
AU - Wurpel, George W.H.
AU - Bonn, Mischa
AU - van der Horst, Michael A.
AU - Hellingwerf, Klaas J.
AU - Matsunaga, Soichiro
AU - Yamada, Taro
AU - Kawai, Maki
N1 - Funding Information:
This study was financially supported in part by RIKEN President Discretionary Fund (2004–2006) and Grants-in-Aid for Scientific Research on Promotion of Novel Interdisciplinary Fields Based on Nanotechnology and Materials from Ministry of Education, Culture, Sports, Science and Technology of Japan. One of the authors (I.I.R.) thanks to Japan Society for the Promotion of Science (JSPS) for the financial support. M.B. acknowledges support from the Young Academy of the Royal Dutch Academy of Sciences.
PY - 2009/4/6
Y1 - 2009/4/6
N2 - The adsorption of photoactive yellow protein (PYP) on a Au(1 1 1) surface and its fluorescence activity have been studied by electrochemical scanning tunneling microscopy (EC-STM) and fluorescence photometry. A stable, densely packed protein layer was observed after protein immobilization onto a Au(1 1 1) surface modified with a mixture of 3-mercaptopropanoic acid (3-MPA) and 11-mercaptoundecanoic acid (11-MUA) and subsequent formation of the amide bond with the use of N-hydroxysuccinimide and carbodiimide. Fluorescence photometry data indicate that covalent binding of PYP to the functionalized Au(1 1 1) surface does not interfere with the fluorescence properties of the native protein.
AB - The adsorption of photoactive yellow protein (PYP) on a Au(1 1 1) surface and its fluorescence activity have been studied by electrochemical scanning tunneling microscopy (EC-STM) and fluorescence photometry. A stable, densely packed protein layer was observed after protein immobilization onto a Au(1 1 1) surface modified with a mixture of 3-mercaptopropanoic acid (3-MPA) and 11-mercaptoundecanoic acid (11-MUA) and subsequent formation of the amide bond with the use of N-hydroxysuccinimide and carbodiimide. Fluorescence photometry data indicate that covalent binding of PYP to the functionalized Au(1 1 1) surface does not interfere with the fluorescence properties of the native protein.
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U2 - 10.1016/j.cplett.2009.02.067
DO - 10.1016/j.cplett.2009.02.067
M3 - Article
AN - SCOPUS:62949246806
VL - 472
SP - 113
EP - 117
JO - Chemical Physics Letters
JF - Chemical Physics Letters
SN - 0009-2614
IS - 1-3
ER -