scholarly journals Covalent Protein Immobilization onto Muscovite Mica Surface with a Photocrosslinker

Minerals ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 464
Author(s):  
Anastasia A. Valueva ◽  
Ivan D. Shumov ◽  
Anna L. Kaysheva ◽  
Irina A. Ivanova ◽  
Vadim S. Ziborov ◽  
...  
Keyword(s):  
Protein Immobilization ◽  
Mass Spectrometry Analysis ◽  
Biological Macromolecules ◽  
Spectrometry Analysis ◽  
Force Microscopy ◽  
Amino Silane ◽  
Research Areas ◽  
Atomic Force ◽  
Muscovite Mica ◽  
Peroxidase Enzyme

Muscovite mica with an amino silane-modified surface is commonly used as a substrate in atomic force microscopy (AFM) studies of biological macromolecules. Herein, the efficiency of two different protein immobilization strategies employing either (N-hydroxysuccinimide ester)-based crosslinker (DSP) or benzophenone-based photoactivatable crosslinker (SuccBB) has been compared using AFM and mass spectrometry analysis. Two proteins with different physicochemical properties—human serum albumin (HSA) and horseradish peroxidase enzyme protein (HRP)—have been used as model objects in the study. In the case of HRP, both crosslinkers exhibited high immobilization efficiency—as opposed to the case with HSA, when sufficient capturing efficiency has only been observed with SuccBB photocrosslinker. The results obtained herein can find their application in commonly employed bioanalytical systems and in the development of novel highly sensitive chip-based diagnostic platforms employing immobilized proteins. The obtained data can also be of interest for other research areas in medicine and biotechnology employing immobilized biomolecules.

Highly sensitive protein detection by combination of atomic force microscopy fishing with charge generation and mass spectrometry analysis

FEBS Journal ◽  
2014 ◽  
Vol 281 (20) ◽  
pp. 4705-4717 ◽  
Author(s):  
Yuri D. Ivanov ◽  
Tatyana Pleshakova ◽  
Krystina Malsagova ◽  
Andrey Kozlov ◽  
Anna Kaysheva ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Atomic Force Microscopy ◽  
Protein Detection ◽  
Mass Spectrometry Analysis ◽  
Charge Generation ◽  
Spectrometry Analysis ◽  
Force Microscopy ◽  
Atomic Force ◽  
Highly Sensitive

scholarly journals Self-assembly of a terbium(III) 1D coordination polymer on mica

2019 ◽  
Vol 10 ◽  
pp. 2440-2448 ◽  
Author(s):  
Quentin Evrard ◽  
Giuseppe Cucinotta ◽  
Felix Houard ◽  
Guillaume Calvez ◽  
Yan Suffren ◽  
...  
Keyword(s):  
Self Assembly ◽  
Water Adsorption ◽  
Bulk Material ◽  
Molecular Organization ◽  
Suitable Candidate ◽  
Force Microscopy ◽  
Atomic Force ◽  
1D Coordination Polymer ◽  
Muscovite Mica ◽  
Intermediate Value

The terbium(III) ion is a particularly suitable candidate for the creation of surface-based magnetic and luminescent devices. In the present work, we report the epitaxial growth of needle-like objects composed of [Tb(hfac)3·2H2O] n (where hfac = hexafluoroacetylacetonate) polymeric units on muscovite mica, which is observed by atomic force microscopy. The needle-like shape mimics the structure observed in the crystalline bulk material. The growth of this molecular organization is assisted by water adsorption on the freshly air-cleaved muscovite mica. This deposition technique allows for the observation of a significant amount of nanochains grown along three preferential directions 60° apart from another. The magnetic properties and the luminescence of the nanochains can be detected without the need of surface-dedicated instrumentation. The intermediate value of the observed luminescence lifetime of the deposits (132 µs) compared to that of the bulk (375 µs) and the CHCl3 solution (13 µs) further reinforces the idea of water-induced growth.

Structure, Flexibility and Intramolecular Forces Observed on Individual Proteins Using Afm

1999 ◽  
Vol 5 (S2) ◽  
pp. 996-997
Author(s):  
Daniel J. Müller ◽  
Andreas Engel
Keyword(s):  
Aqueous Solution ◽  
Short Range ◽  
Biological Macromolecules ◽  
Force Microscopy ◽  
Atomic Force ◽  
Lateral Forces ◽  
Local Reduction ◽  
Electrostatic Double Layer ◽  
Structure Flexibility ◽  
Intramolecular Forces

Atomic force microscopy (AFM) allows the surfaces of native biological macromolecules to be imaged in aqueous solution with submolecular resolution. Short range forces govern the interactions between the AFM tip and the sample and produce the submolecular information of high resolution topographs. In contrast, the long range electrostatic double-layer (EDL) force can be adjusted by pH and electrolytes to distribute the force applied to the AFM tip over a large sample area [1]. As demonstrated on fragile biological samples, adjustment of the electrolyte solution results in a local reduction of both vertical and lateral forces between the AFM tip and proteineous substructures. Consequently, the deformation of the native protein is minimized and polypeptide loops of individual proteins were imaged in aqueous solution with a lateral resolution < 5 Åand a vertical resolution < 1 Å (Fig. 1).

Atomic force microscopy of mica surface after ion replacement

1991 ◽  
Vol 49 ◽  
pp. 628-629 ◽  
Author(s):  
B. L. Dixon Northern ◽  
Y. L. Chen ◽  
J.N. Israelachvili ◽  
J.A.N. Zasadzinski
Keyword(s):  
Surface Charge ◽  
Isomorphous Substitution ◽  
Potassium Ions ◽  
Force Microscopy ◽  
Atomic Force ◽  
Multivalent Ions ◽  
Monovalent Ions ◽  
Muscovite Mica ◽  
Negative Surface ◽  
Negative Surface Charge

Atomic Force Microscope (AFM), is the newest, and potentially most powerful of the scanning probe microscopes. The (AFM) is capable of resolutions approaching atomic dimensions on ideal surfaces. One of the favorite such surfaces is that of mica. Muscovite mica has a platelike structure consisting of an octahedral alumina sheet sandwiched by two tetrahedral silicate sheets. As a result of this structure, mica cleaves readily along a plane leaving a molecularly smooth surface. Because of the isomorphous substitution of the tetravalent silicon by trivalent aluminium, mica has an excess negative surface charge.This negative surface charge of 2.1-1014 charges per cm2 is neutralized by an equal number of positive monovalent ions, mainly potassium ions. The ion-exchangable surface ions of mica, in aqueous solution, can be readily replaced by other monovalent or multivalent ions. This ion exchange alters the surface of the mica. We then follow these changes by imaging with the AFM in air.

Large Scale Anomalous Patterns of Muscovite Mica Discovered by Atomic Force Microscopy

2015 ◽  
Vol 7 (16) ◽  
pp. 8699-8705 ◽  
Author(s):  
Feng Zhang ◽  
Ping Zhang ◽  
Jiahua Hou ◽  
Xiaoling Yun ◽  
Wanrong Li ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Large Scale ◽  
Force Microscopy ◽  
Atomic Force ◽  
Muscovite Mica

scholarly journals Atomic force microscopy as an advanced tool in neuroscience

2015 ◽  
Vol 6 (1) ◽  
pp. 117-130 ◽  
Author(s):  
Maja Jazvinšćak Jembrek ◽  
Goran Šimić ◽  
Patrick R. Hof ◽  
Suzana Šegota
Keyword(s):  
Mechanical Properties ◽  
Atomic Force Microscopy ◽  
Physical Structure ◽  
Neuronal Morphology ◽  
Specific Information ◽  
Force Microscopy ◽  
Research Areas ◽  
Atomic Force ◽  
Neuronal Membranes ◽  
Imaging Mode

AbstractThis review highlights relevant issues about applications and improvements of atomic force microscopy (AFM) toward a better understanding of neurodegenerative changes at the molecular level with the hope of contributing to the development of effective therapeutic strategies for neurodegenerative illnesses. The basic principles of AFM are briefly discussed in terms of evaluation of experimental data, including the newest PeakForce Quantitative Nanomechanical Mapping (QNM) and the evaluation of Young’s modulus as the crucial elasticity parameter. AFM topography, revealed in imaging mode, can be used to monitor changes in live neurons over time, representing a valuable tool for high-resolution detection and monitoring of neuronal morphology. The mechanical properties of living cells can be quantified by force spectroscopy as well as by new AFM. A variety of applications are described, and their relevance for specific research areas discussed. In addition, imaging as well as non-imaging modes can provide specific information, not only about the structural and mechanical properties of neuronal membranes, but also on the cytoplasm, cell nucleus, and particularly cytoskeletal components. Moreover, new AFM is able to provide detailed insight into physical structure and biochemical interactions in both physiological and pathophysiological conditions.

scholarly journals Atomic force microscopy fishing of gp120 on immobilized aptamer and its mass spectrometry identification

2015 ◽  
Vol 61 (3) ◽  
pp. 363-372 ◽  
Author(s):  
N.S. Bukharina ◽  
Yu.D. Ivanov ◽  
T.O. Pleshakova ◽  
P.A. Frantsuzov ◽  
E.Yu. Andreeva ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Atomic Force Microscopy ◽  
Protein Detection ◽  
Target Protein ◽  
Mass Spectrometry Analysis ◽  
Molecular Probe ◽  
Bulk Solution ◽  
Force Microscopy ◽  
Atomic Force ◽  
Mass Spectrometry Identification

A method of atomic force microscopy-based fishing (AFM fishing) has been developed for protein detection in the analyte solution using a chip with an immobilized aptamer. This method is based on the biospecific fishing of a target protein from a bulk solution onto the small AFM chip area with the immobilized aptamer to this protein used as the molecular probe. Such aptamer-based approach allows to increase an AFM image contrast compared to the antibody-based approach. Mass spectrometry analysis used after the biospecific fishing to identify the target protein on the AFM chip has proved complex formation. Use of the AFM chip with the immobilized aptamer avoids interference of the antibody and target protein peaks in a mass spectrum.

Sign in / Sign up

Export Citation Format

Share Document