Atomic Force Microscopy of Protein Complexes

Kiselyova, Olga I.; Yaminsky, I.

doi:10.1385/1-59259-647-9:217

Cited by 16 publications

(20 citation statements)

References 25 publications

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“…At the same time, in the InjI mode experiments the characteristic changes of the potential were registered (Fig. 8B, curves 3,4,5). In this experimental series, the changes of the potential varied between 20 and 100 V. As in the experiments with deionized water, a cyclic type of changes of the potential U(t) (between 20 and 100 V) was observed upon repeated injection of HSA solution at 10 À14 M concentration.…”

Section: Concentration Mmentioning

confidence: 53%

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

et al. 2014

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An approach combining atomic force microscopy (AFM) fishing and mass spectrometry (MS) analysis to detect proteins at ultra‐low concentrations is proposed. Fishing out protein molecules onto a highly oriented pyrolytic graphite surface coated with polytetrafluoroethylene film was carried out with and without application of an external electric field. After that they were visualized by AFM and identified by MS. It was found that injection of solution leads to charge generation in the solution, and an electric potential within the measuring cell is induced. It was demonstrated that without an external electric field in the rapid injection input of diluted protein solution the fishing is efficient, as opposed to slow fluid input. The high sensitivity of this method was demonstrated by detection of human serum albumin and human cytochrome b5 in 10−17–10−18 m water solutions. It was shown that an external negative voltage applied to highly oriented pyrolytic graphite hinders the protein fishing. The efficiency of fishing with an external positive voltage was similar to that obtained without applying any voltage.

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Section: Concentration Mmentioning

confidence: 53%

“…Atomic force microscopy (AFM) is one of such molecular detectors. The AFM device enables protein molecules that are located on the surface to be visualized and registered [2][3][4]. Another major factor that exerts influence on the analytical system sensitivity is the efficiency of the protein delivery from solution to the sensor surface.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2014

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“…where D is the "true" diameter, r is the tip radius, and d is the measured diameter at half vertical height (35). DNPH Immunoassay for Carbonyl Groups-1 mM H 2 O 2 was added to the aggregated, airfuged, and washed A␤(1-42) pellets, and 2-l samples were taken immediately (time zero) and again after 48, 72, or 144 h and added to 6 l of 10 mM DNPH in 6 M guanidine hydrochloride.…”

Section: Experimental Proceeduresmentioning

confidence: 99%

β-Amyloid Fibrils in Alzheimer Disease Are Not Inert When Bound to Copper Ions but Can Degrade Hydrogen Peroxide and Generate Reactive Oxygen Species

Mayes

Tinker-Mill

Kolosov

et al. 2014

Journal of Biological Chemistry

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Background: Metal-associated ␤-amyloid (A␤) aggregates are implicated in the pathogenesis of Alzheimer disease. Results: Copper bound A␤(1-42) aggregates, including fibrils, degrade hydrogen peroxide, forming hydroxyl radicals and carbonyls. Conclusion: Copper-bound A␤ fibrils can retain redox activity. Significance: A␤ fibrils bound to copper are not inert end points and may be a source of oxidative stress in the Alzheimer brain.

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“…The presence in the structure of muscovite layers of potassium ions determines the separation of sheets of mica, consisting of double layers of SiO 4 tetrahedra. Interlayer potassium ions extremely easily replaced with water molecules 26,27 , making space for adsorption of protein. The oxygen atoms of the SiO 4 tetrahedra at interaction with water solutions of various substances, including proteins acquire a negative charge.…”

Section: Discussionmentioning

confidence: 99%

Surface-Dependent Differences in the Adsorption of Pancreatic and Microbial Ribonucleases Visualized by Atomic Force Microscopy

Коновалова¹,

Kalacheva²,

Черепнев³

et al. 2016

Biosci., Biotech. Res. Asia

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A comparative study of the physical adsorption of RNAse A and RNAse Bacillus pumilis onto a negatively charged surface of mica, a hydrophobic surface of pyrolytic graphite and a surface of lipid layers of dipalmitoylphosphatidylcholine (DPPC) was performed by atomic force microscopy. It was found that microbial RNAse, unlike RNAse A, 1) is adsorbed onto the negatively charged surface of mica in the form of monomers and dimers; 2) exhibits enhanced tropism to the hydrophobic surface of pyrolytic graphite; 3) modifies morphotopography and thickness of the lipid bilayer of DPPC. The detected surface-dependent differences in adsorption of RNAses are consistent with the features of their structure and cytotoxic properties.

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Atomic Force Microscopy of Protein Complexes

Cited by 16 publications

References 25 publications

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

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

β-Amyloid Fibrils in Alzheimer Disease Are Not Inert When Bound to Copper Ions but Can Degrade Hydrogen Peroxide and Generate Reactive Oxygen Species

Surface-Dependent Differences in the Adsorption of Pancreatic and Microbial Ribonucleases Visualized by Atomic Force Microscopy

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