Use of Surface Plasmon Resonance Coupled with Mass Spectrometry Reveals an Interaction between the Voltage-Gated Sodium Channel Type X α-Subunit and Caveolin-1

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• 作者：Elisabet hman ; Anna Nilsson ; Alexandra Madeira ; Benita Sjgren ; Per E. Andrn ; Per Svenningsson
• 刊名：Journal of Proteome Research
• 出版年：2008
• 出版时间：December 5, 2008
• 年：2008
• 卷：7
• 期：12
• 页码：5333-5338
• 全文大小：161K
• 年卷期：v.7,no.12(December 5, 2008)
• ISSN：1535-3907

文摘

The combination of surface plasmon resonance and mass spectrometry is emerging as a sensitive tool for the elucidation of protein−protein interactions. With the use of surface plasmon resonance-mass spectrometry, peptides, and brain extracts, we now report a novel interaction between the voltage-gated sodium channel type X α-subunit and caveolin-1, the central protein controlling caveolae formation. Surface plasmon resonance binding analyses show that this interaction involves amino acids 85−103 of voltage-gated sodium channel type X α-subunit and amino acids 81−100 of caveolin-1, a known scaffolding domain of caveolin-1. It is anticipated that the surface plasmon resonance-mass spectrometry approach utilized in this study will be important for the elucidation of protein−protein network analysis in native tissues including the brain.