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Covalent anchoring of proteins onto gold‐directed NHS‐terminated self‐assembled monolayers in aqueous buffers: SFM images of clathrin cages and triskelia
Author(s) -
Wagner Peter,
Kernen Peter,
Hegner Martin,
Ungewickell Ernst,
Semenza Giorgio
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01296-2
Subject(s) - monolayer , covalent bond , aqueous solution , self assembly , anchoring , clathrin , chemistry , self assembled monolayer , nanotechnology , materials science , organic chemistry , biochemistry , endocytosis , receptor , structural engineering , engineering
N ‐Hydroxysuccinimide‐terminated self‐assembled monolayers with linear (CH 2 ) 10 chains were prepared on ultraflat Au(111) surfaces from dithio bis (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.