Detection and localization of individual antibody-antigen recognition events by atomic force microscopy
作者： P. Hinterdorfer , W. Baumgartner , H. J. Gruber , K. Schilcher , H. Schindler
关键词: Human serum albumin 、 Molecular recognition 、 Microscopy 、 Binding site 、 Stereochemistry 、 Microscope 、 Serum albumin 、 Molecule 、 Biophysics 、 Polyclonal antibodies 、 Chemistry
摘要: A methodology has been developed for the study of molecular recognition at level single events and localization sites on biosurfaces, in combining force microscopy with by specific ligands. For this goal, a sensor was designed covalently linking an antibody (anti-human serum albumin, polyclonal) via flexible spacer to tip microscope. This permitted detection antibody-antigen signals unique shape unbinding 244 +/- 22 pN. Analysis revealed that observed forces originate from dissociation individual Fab fragments human albumin molecule. The two were found bind independently equal probability. linkage provided 6-nm dynamical reach binding, rendering binding probability high, 0.5 encounter times 60 ms. fast reliable antigenic during lateral scans positional accuracy 1.5 nm. It is indicated promise characterizing rate constants kinetics complexes mapping biosurfaces such as membranes.
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