Reduction of nonspecific binding proteins to self-assembled monolayer on gold surface

• Published in: Bioorganic & medicinal chemistry Vol. 14; no. 2; pp. 537 - 543
• Main Authors: Furuya, Minoru, Haramura, Masayuki, Tanaka, Akito
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 15-01-2006; Elsevier Science
• Subjects: Animals; Biological and medical sciences; Biosensors; Biotechnology; Brain; Escherichia coli - chemistry; FK506; FKBP12; Fundamental and applied biological sciences. Psychology; Gold; Methods. Procedures. Technologies; Nonspecific binding proteins; Rats; Surface Plasmon Resonance; Surface Properties; Tacrolimus - chemistry; Tacrolimus Binding Protein 1A - chemistry; Various methods and equipments; Nonspecific binding proteins; Surface plasmon resonance; FK506; FKBP12; Self-assembled layer; Self assembly; Monolayer; Escherichia; Gold; Chemical stability; Glass; Transition metal; System on a chip; Surface structure; Ethylene oxide polymer; Binding protein; Tacrolimus; Bacteria; Miniaturization; Enterobacteriaceae; Modified material
• ISSN: 0968-0896; 1464-3391
• DOI: 10.1016/j.bmc.2005.09.030

Application of
1 on gold surface enabled adequate estimation of
K
d value between FK506 and FKBP12 by SPR not only using purified FKBP12 but using
Escherichia coli lysate expressing FKBP12.
We developed a gold coated glass chip bearing a poly(ethyleneglycol) (PEG) type compound as hydrophilic spacer for surface plasmon resonance studies, which enabled adequate estimation of
K
d value between FK506 and FKBP12 not only using purified FKBP12 (
K
d
=
22
nM) but also using
Escherichia coli lysate expressing FKBP12 (
K
d
=
15
nM). These results indicated effectiveness of the PEG spacer for reduction of nonspecific interactions. Chemical stability and simple surface-structure of the novel chip are also attractive.