Characterization of surface-confined alpha-synuclein by surface plasmon resonance measurements.
Urea-driven denaturation and renaturation of surface-bound alpha-synuclein are monitored by surface plasmon resonance (SPR) spectroscopy. The differential SPR angle shift (Delta Theta(SPR))(Net) enables us to estimate the Gibbs free energy change (DeltaG(o)) for the denaturation of the supported alpha-synuclein. DeltaG(o) for the denaturation of the supported alpha-synuclein, which is indirectly related to its biological activity can be increased significantly by the mixed self-assembled monolayers of 11-mercaptoundecanoic acid and 1,6-hexanedithiol. These SPR measurements of surface-bound biomolecules suggested herein can be further utilized to design effective biological scaffold for biosensor, biocatalyst, and possible diagnosis.
Kang
Taewook
T
School of Chemical and Biological Engineering, Institute of Chemical Processes, Seoul National University, Shillim, Kwanak, Seoul 151-742, Korea.
Hong
Surin
S
Kim
Hyun Jin
HJ
Moon
Jungwoo
J
Oh
Seogil
S
Paik
Seung R
SR
Yi
Jongheop
J
D020099:Coated Materials, Biocompatible; D011489:Protein Denaturation; D011994:Recombinant Proteins / Q000737:chemistry; D020349:Surface Plasmon Resonance; D013816:Thermodynamics; D014508:Urea; D051844:alpha-Synuclein / Q000737:chemistry*
D020099:Coated Materials, Biocompatible; D011994:Recombinant Proteins; D051844:alpha-Synuclein; D014508:Urea