Probing single molecule interactions by AFM using bio-functionalized dendritips

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• 作者：Eric Jauvert^a ; ^b ; ^c ; ^d ; ^e ; ¹  ; [Author Vitae] ; Etienne Dague^b ; ^c ; ^d ; ^e ; ¹  ; [Author Vitae] ; Marjorie Sé ; verac^f ; ^g  ; [Author Vitae] ; Laurence Ressier^a  ; [Author Vitae] ; Anne-Marie Caminade^f ; ^g  ; [Author Vitae] ; Jean-Pierre Majoral^f ; ^g  ; [Author Vitae] ; Emmanuelle Tré ; visiol^d ; ^e ; ^h ; ⁱ ; ^j ; ^{emmanuelle.trevisiol@insa-toulouse.fr}  ; [Author Vitae]
• 关键词：AFM tip functionalization ; Phosphorus dendrimers ; Single molecule force spectroscopy (SMFS) ; Molecular recognition ; Antigen/antibody interaction
• 刊名：Sensors and Actuators B ; Chemical
• 出版年：2012
• 期刊代码：161_09254005
• 类别：et
• 出版时间：20 June, 2012
• 卷：168
• 期：Complete
• 页码：436-441
• 文件大小：683 K

摘要

A new strategy for AFM (atomic force microscopy) tip functionalization based on the use of aldehyde-phosphorus dendrimers for the immobilization of biomolecules such as proteins (e.g. antibodies) is presented. Firstly functionalized with amino groups, the tips are reacted with dendrimers leading to dendrimer-activated tips (so-called dendritips). Free aldehyde functions on the dendrimer are therefore available to react with amino-functions present on every protein and many biomolecules. Using biofunctionalized-dendritip, single molecule force interactions between glutathione-S-transferase (GST) and its cognate antibody immobilized on dendritips (67 卤 11 pN for single interaction) were probed by AFM spectroscopy. The specificity of our measurements was demonstrated by performing blocking tests resulting in the loss of interactions.