Characterization of surface-confined α-synuclein by surface plasmon resonance measurements

被引：15
|
作者：
Kang, T [1 ]
Hong, S [1 ]
Kim, HJ [1 ]
Moon, J [1 ]
Oh, S [1 ]
Paik, SR [1 ]
Yi, J [1 ]
机构：
[1] Seoul Natl Univ, Sch Chem & Biol Engn, Inst Chem Proc, Seoul 151742, South Korea
来源：
LANGMUIR | 2006年 / 22卷 / 01期
关键词：
D O I：
10.1021/la052276w
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
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 (Delta G degrees) for the denaturation of the supported alpha-synuclein. Delta G degrees 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.
引用
收藏
页码：13 / 17
页数：5
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