Covalent anchoring of proteins onto gold‐directed NHS‐terminated self‐assembled monolayers in aqueous buffers: SFM images of clathrin cages and triskelia

FEBS Letters

Hegner, Martin¹  Wagner, Peter¹  Semenza, Giorgio¹  Kernen, Peter¹  Ungewickell, Ernst² 

[1] Department of Biochemistry, Swiss Federal Institute of Technology, ETH Zentrum, CH 8092 Zurich, Switzerland;Department of Pathology, Washington University, St. Louis, MO 63110, USA

关键词: Atomic force microscopy;    Scanning force microscopy;    Gold;    Self-assembled monolayer;    N-Hydroxysuccinimide;    Clathrin;    Triskelion;    SPM;    scanning probe microscopy;    SFM;    scanning force microscopy;    STM;    scanning tunneling microscopy;    SAM;    self-assembled monolayer;    NHS;    N-Hydroxysuccinimide;    TSG;    template-stripped gold;    DSU;    dithiobis(succinimidylundecanoate);    HOPG;    highly oriented pyrolytic graphite;   

DOI  :  10.1016/0014-5793(94)01296-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

N-Hydroxysuccinimide-terminated self-assembled monolayers with linear (CH₂)₁₀ chains were prepared on ultraflat Au(111) surfaces from dithiobis(succinimidylundecanoate). These monolayers, which are covalently chemisorbed to gold via thiolate bonds, form a highly reactive amino-group specific carpet at the liquid—solid interface. Proteins bind to it covalently in aqueous buffers under mild conditions; this provides a (general) procedure for protein immobilization for scanning probe microscopy. Using this technique, we have obtained what we believe are the first scanning force microscopy images of clathrin cages and of their in situ disassembly, yielding typical triskelia under non-denaturing conditions.

【 授权许可】

Unknown