Substructures high resolution imaging of individual IgG and IgM antibodies with piezoelectric tuning fork atomic force microscopy

Makky, Ali; Berthelot, Thomas; Féraudet-Tarisse, Cécile; Volland, Hervé; Viel, Pascal; Polesel-Maris, Jérôme

doi:10.1016/j.snb.2011.12.077

Cited by 33 publications

(25 citation statements)

References 43 publications

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“…11 shows local stiffness measurements between two hinges of a concave membrane ranging from 0,6 to 3 N/m. The oscillation amplitude of the tuning fork is non-destructive, and estimated around 700 pm using a method described in [24]. Repeated measurements on the same point were found to fall within 5 % of the same value, on a sample size of a dozen.…”

Section: Resultsmentioning

confidence: 96%

Robotic in situ stiffness cartography of InP membranes by dynamic force sensing

Abrahamians

Sauvet

Polesel-Maris

et al. 2013

2013 IEEE/RSJ International Conference on Intelligent Robots and Systems

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Typical methods of measuring mechanical properties at the micro-scale are destructive, and do not allow proper characterisation on resonant MEMS/NEMS. In this paper, a cartography of local stiffness variations on a suspended micromembrane is established for the first time, by a tuning-forkbased dynamic force sensor inside a SEM. Experiments are conducted on InP membranes 200nm thin, using a 9-DoF nanomanipulation system, complemented with virtual reality and automation tools. Results provide stiffness values ranging from 0.6 to 3 N/m on a single sample.

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Section: Resultsmentioning

confidence: 96%

Robotic in situ stiffness cartography of InP membranes by dynamic force sensing

Abrahamians

Sauvet

Polesel-Maris

et al. 2013

2013 IEEE/RSJ International Conference on Intelligent Robots and Systems

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“…93 Usually used papers have particle retention ranging from 2.5 to 40 mm. 128,131,132 Thus, antibodies (about 24 nm lateral) 133 or enzymes easily go through the ber lattice. In contrast, 0.5 micrometer-scale particles 134,135 have size approaching particle retention values and are thereby more easily retained on the surface.…”

Section: Physical Methodsmentioning

confidence: 99%

Cellulose: from biocompatible to bioactive material

2014

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International audienceSince the papyri, cellulose has played a significant role in human culture, especially as paper. Nowadays, this ancient product has found new scientific applications in the expanding sector of paper-based technology. Among paper-based devices, paper-based biosensors raise a special interest. The high selectivity of biomolecules for target analytes makes these sensors efficient. Moreover, simple paper-based detection devices do not require hardware or specific technical skill. They are inexpensive, rapid, user-friendly and therefore highly promising for providing resource-limited settings with point-of-care diagnostics. The immobilization of biomolecules onto cellulose is a key step in the development of these sensing devices. Following an overview of cellulose structural features and physicochemical properties, this article reviews current techniques for the immobilization of biomolecules on paper membranes. These procedures are categorized into physical, biological and chemical approaches. There is no universal method for biomolecule immobilization. Thus, for a given paper-based biochip, each strategy can be considered

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“…We used a custom homebuilt AFM microscope to drive the tuning fork probe in amplitude modulation AFM and for BFS measurements. The system and the scanning probe preparation were already described in detail in previous works (Makky et al ., ; Polesel‐Maris et al ., ). Figure detailed the set‐up used in this work where we introduced a new fluidic cell to control the liquid interface.…”

Section: Methodsmentioning

confidence: 99%

“…Hence, in the aim to improve the effectiveness of self‐sensing probe in biological applications, we have recently developed a new scanning probe based on a quartz piezoelectric tuning fork scanning probe with a millimeter‐long tip, and we have demonstrated its efficiency on submolecular resolution of two types of antibodies (IgG and IgM) in air (Makky et al ., ). Moreover, we have studied by biochemical force spectroscopy (BFS) in buffer solution, the non‐specific interaction and stretching of bovine serum albumin proteins (Polesel‐Maris et al ., ) with various chemical functionalities grafted onto a carbon etched tip.…”

Section: Introductionmentioning

confidence: 97%

Piezoelectric tuning fork probe for atomic force microscopy imaging and specific recognition force spectroscopy of an enzyme and its ligand

Makky¹,

Viel²,

Chen

et al. 2013

J of Molecular Recognition

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Piezoelectric quartz tuning fork has drawn the attention of many researchers for the development of new atomic force microscopy (AFM) self-sensing probes. However, only few works have been done for soft biological materials imaging in air or aqueous conditions. The aim of this work was to demonstrate the efficiency of the AFM tuning fork probe to perform high-resolution imaging of proteins and to study the specific interaction between a ligand and its receptor in aqueous media. Thus, a new kind of self-sensing AFM sensor was introduced to realize imaging and biochemical specific recognition spectroscopy of glucose oxidase enzyme using a new chemical functionalization procedure of the metallic tips based on the electrochemical reduction of diazonium salt. This scanning probe as well as the functionalization strategy proved to be efficient respectively for the topography and force spectroscopy of soft biological materials in buffer conditions.

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Substructures high resolution imaging of individual IgG and IgM antibodies with piezoelectric tuning fork atomic force microscopy

Cited by 33 publications

References 43 publications

Robotic in situ stiffness cartography of InP membranes by dynamic force sensing

Robotic in situ stiffness cartography of InP membranes by dynamic force sensing

Cellulose: from biocompatible to bioactive material

Piezoelectric tuning fork probe for atomic force microscopy imaging and specific recognition force spectroscopy of an enzyme and its ligand

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